Novel targets for herbicides and transgenic plants resistant to said herbicides

ABSTRACT

The invention concerns novel enzymes having an arogenate dehydrogenase activity, in particular arogenate dehydrogenase enzymes of plants, and the genes encoding said enzymes. The inventive arogenate dehydrogenase enzymes catalyze the last stage of the metabolic pathway of tyrosine biosynthesis, and constitute, as such, potential targets of herbicides. Hence the invention also concerns a method for identifying herbicide compounds targeting said enzymes, said herbicide compounds preventing tyrosine biosynthesis by being fixed on said enzymes. The invention further concerns transgenic plants tolerant to herbicide compounds targeting an enzyme involved in the tyrosine biosynthesis pathway, in particular an enzyme involved in the transformation of L-tyrosine prephenate, in particular an arogenate dehydrogenase enzyme. Said plants become tolerant by expression in their tissues of a prephenate dehydrogenase enzyme, said enzyme being insensitive to said herbicide compounds and enabling the plant to synthetize tyrosine despite being treated with said herbicide compounds.

[0001] The present invention relates to novel enzymes having arogenate dehydrogenase activity, in particular plant arogenate dehydrogenase enzymes, and also to the genes encoding these enzymes. The arogenate hydrogenase enzymes according to the invention catalyze the final step in the metabolic pathway of tyrosine biosynthesis and, in this respect, constitute potential targets for herbicides. The present invention therefore also relates to a method for identifying herbicidal compounds having these enzymes as a target, said herbicidal compounds preventing tyrosine biosynthesis by attaching to said enzymes. The invention also relates to transgenic plants tolerant to herbicidal compounds having as a target an enzyme involved in the biosynthetic pathway for tyrosine, in particular an enzyme involved in the conversion of prephenate to L-tyrosine, in particular an arogenate dehydrogenase enzyme. These plants become tolerant by expression, in their tissues, of a prephenate dehydrogenase enzyme, this enzyme being insensitive to said herbicidal compounds and enabling the plant to synthesize tyrosine despite treatment with said herbicidal compounds.

[0002] The biosynthetic pathway for aromatic amino acids constitutes a metabolic pathway which is essential for plants, bacteria and fungi. In addition to the biosynthesis of tyrosine, phenylalanine and tryptophan, this metabolic pathway plays an essential role in the production of many secondary aromatic metabolites involved in processes such as plant-microbe interactions, the biosynthesis of structural biopolymers such as lignin and suberin, hormone synthesis, or quinone synthesis. Among all the living organisms which have this metabolic pathway, two pathways have been identified for converting prephenate to tyrosine (FIG. 1; Stenmark et al., 1974). In most chlorophyll-containing bacteria, some microorganisms and most plants, L-tyrosine is synthesized via the arogenate pathway (Abou-Zeid et al., 1995; Byng et al., 1981; Connely and Conn 1986; Frazel and Jensen 1979; Gaines et al., 1982; Hall et al., 1982; Keller et al., 1985; Mayer et al., 1985). In this pathway, the prephenate is transaminated to arogenate by a specific transaminase, prephenate aminotransferase (EC 2.6.1.57), and the arogenate is then converted to L-tyrosine by an arogenate dehydrogenase (EC 1.3.1.43; ADH on FIG. 1). In a different manner, in organisms such as the bacterium Escherichia coli or yeast, the prephenate is, initially, converted to p-hydroxyphenylpyruvate by a prephenate dehydrogenase (EC 1.3.1.12, EC 1.3.1.13), which p-hydroxyphenylpyruvate is transaminated to L-tyrosine (Lingens et al., 1967). By virtue of its role in the biosynthetic pathway for tyrosine in plants, the arogenate dehydrogenase enzyme constitutes a potential target for novel herbicides.

[0003] Other enzymes involved in this metabolic pathway already constitute major herbicide targets. Mention may, for example, be made of the enzyme 5-enolpyruvyl-shikimate 3-phosphate synthase (EPSPS), involved upstream of prephenate synthesis, which is the target for the total herbicide glyphosate. Mention may also be made of the enzyme p-hydroxyphenylpyruvate dioxygenase (HPPD) involved in the conversion of p-hydroxyphenylpyruvate to homogentisate. HPPD is the target for novel families of herbicides, the activity of which leads to bleaching of the leaves (Schulz et al., 1993; Secor 1994). These herbicides are in particular isoxazoles (EP 418 175, EP 470 856, EP 487 352, EP 527 036, EP 560 482, EP 682 659, U.S. Pat. No. 5,424,276), in particular isoxaflutole, a maize-selective herbicide, diketonitriles (EP 496 630, EP 496 631) in particular 2-cyano-3-cyclopropyl-1-(2-SO₂CH₃-4-CF₃ phenyl)propane-1,3-dione and 2-cyano-3-cyclopropyl-1-(2-SO₂CH₃-4,2,3-Cl₂ phenyl)propane-1,3-dione, triketones (EP 625 505, EP 625 508, U.S. Pat. No. 5,506,195), in particular sulcotrione or mesotrione, or else pyrazolinates.

[0004] One of the advantages of the herbicides having for a target enzymes involved in the metabolic pathways essential to plants is their broad spectrum of activity on plants of distant phylogenetic origins. However, such herbicides also have the major drawback, when they are applied to crops in order to eliminate the undesirable plants or “weeds”, of also acting on the cultivated plants. This drawback can be overcome by using cultivated plants tolerant to said herbicides. Such plants are generally obtained by genetic engineering, by introducing into their genome a gene encoding an enzyme for resistance to said herbicide, in such a way that they overexpress said enzyme in their tissues. To date, three main strategies using genetic engineering have been employed to make plants tolerant to herbicides. The first consists in detoxifying the herbicide by transforming the plant with a gene encoding a detoxification enzyme. This enzyme converts the herbicide, or its active metabolite, to nontoxic degradation products, such as, for example, the enzymes for tolerance to bromoxynil or to basta (EP 242 236, EP 337 899). The second strategy consists in transforming the plant with a gene encoding the target enzyme mutated in such a way that it is less sensitive to the herbicide, or its active metabolite, such as, for example, the enzymes for tolerance to glyphosate (EP 293 356, Padgette S. R. & al., J. Biol. Chem., 266, 33, 1991). The third strategy consists in over-expressing the sensitive target enzyme so as to produce, in the plant, large amounts of target enzyme, if possible much greater than the amount of herbicide entering the plant. This strategy, which has been used to successfully obtain plants tolerant to HPPD inhibitors (WO 96/38567), makes it possible to maintain a sufficient level of functional enzyme despite the presence of its inhibitor.

[0005] The fact that two biosynthetic pathways for L-tyrosine exist in different taxonomic groups, and in particular that the pathway directly converting prephenate to p-hydroxyphenylpyruvate is not found in plants, makes it possible to envision a fourth strategy for making plants tolerant to herbicides. Specifically, in the case of use of a herbicidal compound having as target the arogenate dehydrogenase enzyme in plants, transforming the plants intended to be made tolerant with a gene encoding a bacterial or yeast prephenate dehydrogenase enzyme will enable said plants to synthesize L-tyrosine, and therefore to tolerate the presence of the herbicidal compound despite the inhibition of the arogenate dehydrogenase enzyme by said herbicidal compound. This novel strategy therefore consists in creating, in the plants intended to be made resistant, a bypassing of the natural metabolic pathway for tyrosine biosynthesis, which pathway uses the arogenate dehydrogenase enzyme, by artificial implantation in these plants of a novel metabolic pathway for tyrosine biosynthesis, which uses the prephenate dehydrogenase enzyme. Such bypassing allows the plants possessing it, preferably plants of agronomic interest, to tolerate the presence of the herbicidal compound which inhibits the natural metabolic pathway, whereas the plants not possessing this bypassing, in particular the weeds, will be sensitive to said herbicidal compound.

DESCRIPTION

[0006] The present invention therefore relates to novel isolated polynucleotides encoding an enzyme having arogenate dehydrogenase activity. According to the present invention, the term “polynucleotide” is intended to mean a natural or artificial nucleotide sequence which may be of the DNA or RNA type, preferably of the DNA type, in particular double-stranded. The expression “enzymes having arogenate dehydrogenase activity” is intended to mean the enzymes capable of converting arogenate to L-tyrosine. The arogenate dehydrogenase activity is measured by any method which makes it possible either to measure a decrease in the amount of the arogenate substrate, or to measure an accumulation of a product derived from the enzyme reaction, namely L-tyrosine or the cofactor NADPH. In particular, the arogenate dehydrogenase activity can be measured by the method described in example 4.

[0007] According to a particular embodiment of the invention, the polynucleotides encoding an arogenate dehydrogenase enzyme comprise polynucleotides encoding the polypeptide sequence selected from the sequence described in the sequence identifier SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11 or SEQ ID NO: 13. It is well known to those skilled in the art that this definition includes all the polynucleotides which, although comprising nucleotide sequences which are different as a result of the degeneracy of the genetic code, encode the same amino acid sequence, which sequence is represented by the sequence identifiers SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11 or SEQ ID NO: 13.

[0008] The present invention also comprises isolated polynucleotides encoding arogenate dehydrogenase enzymes and capable of hybridizing selectively to one of the polynucleotides described above, or a fragment of these polynucleotides constituting a probe. According to the invention, the expression “polynucleotide capable of hybridizing selectively” is intended to mean the polynucleotides which, by one of the usual methods of the state of the art (Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, Nolan C. ed., New York: Cold Spring Harbor Laboratory Press), hybridize with the polynucleotides above, or with the probes which are derived therefrom, at a level significantly greater than the background noise. The background noise may be associated with the hybridization of other polynucleotides present, for example other cDNAs present in a cDNA library. The level of the signal generated by the interaction between the polynucleotide capable of hybridizing selectively and the polynucleotides defined by the sequences SEQ ID NOS: above according to the invention, or the probes, is generally 10 times, preferably 100 times, more intense than that generated by the interaction with other DNA sequences generating the background noise. The level of interaction can be measured, for example, by labeling the polynucleotides described above or the probes with radioactive elements, such as ³²P. Selective hybridization is generally obtained using very severe conditions for the medium (for example 0.03 M NaCl and 0.03 M sodium citrate at approximately 50° C.-60° C.).

[0009] The invention also comprises isolated polynucleotides encoding arogenate dehydrogenase enzymes, and homologs of the polynucleotides described above. According to the invention, the term “homolog” is intended to mean polynucleotides exhibiting one or more sequence modifications compared to the nucleotide sequences described above and encoding an enzyme with functional arogenate dehydrogenase activity. These modifications may be natural or obtained artificially according to the usual techniques of mutation leading in particular to the addition, deletion or substitution of one or more nucleotides compared to the sequences of the invention. These modifications determine a degree of homology with respect to the sequences described above. Advantageously, the degree of homology will be at least 70% compared to the sequences described, preferably at least 80%, more preferentially at least 90%. The methods for measuring and identifying homologies between nucleic acid sequences are well known to those skilled in the art. Use may, for example, be made of the PILEUP or BLAST programs (Basic Local Alignment Search Tool; Altschul et al., 1993, J. Mol. Evol. 36: 290-300; Altschul et al., 1990, J. Mol. Biol. 215: 403-10; see also http://www.ncbi.nlm.nih.gov/BLAST/).

[0010] The present invention also relates to fragments of the polynucleotides described above. The term “fragment” denotes in particular a fragment of at least 20 nucleotides, in particular of at least 50 nucleotides, and preferably of at least 100 nucleotides. According to a particular embodiment of the invention, the polynucleotide according to the invention is represented by the sequence identifier SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10 or SEQ ID NO: 12.

[0011] The present invention also relates to polynucleotides comprising at least one of the polynucleotides as described above.

[0012] All the polynucleotides described above encode arogenate dehydrogenase enzymes. Consequently, the invention therefore extends to all the arogenate dehydrogenase enzymes encoded by all of these polynucleotides.

[0013] According to a particular embodiment of the invention, the arogenate dehydrogenase enzyme is an enzyme the peptide sequence of which is selected from the sequence described by the sequence identifier SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11 or SEQ ID NO: 13., or a fragment of these sequences. The term “fragment” is intended to mean essentially a biologically active fragment, i.e. a fragment of the sequence of an arogenate dehydrogenase enzyme having the same activity as a complete arogenate dehydrogenase enzyme.

[0014] According to a particular embodiment of the invention, the polynucleotides and the arogenate dehydrogenase enzymes described above originate from plants. More particularly, they originate from plants of the Arabidopsis genus, preferably of the A. thaliana genus, or from plants of the Picea genus, preferably Picea glauca.

[0015] According to another particular embodiment of the invention, the polynucleotides and the arogenate dehydrogenase enzymes described above originate from bacteria. More particularly, they originate from bacteria of the Synechocystis genus.

[0016] The present invention also relates to a chimeric gene comprising, functionally linked to one another, at least one promoter which is functional in a host organism, a polynucleotide encoding an arogenate dehydrogenase enzyme as defined in the present inven- tion, and a terminator element which is functional in this same host organism. The various elements that a chimeric gene may contain are, firstly, elements which regulate the transcription, translation and maturation of proteins, such as a promoter, a sequence encoding a signal peptide or a transit peptide, or a terminator element constituting a polyadenylation signal and, secondly, a polynucleotide encoding a protein. The expression “functionally linked to one another” means that said elements of the chimeric gene are linked to one another in such a way that the functioning of one of these elements is affected by that of another. By way of example, a promoter is functionally linked to a coding sequence when it is capable of affecting the expression of said coding sequence. The construction of the chimeric gene according to the invention and the assembly of its various elements can be carried out using techniques well known to those skilled in the art, in particular those described by Sambrook et al., (1989, Molecular Cloning: A Laboratory Manual, Nolan C. ed., New York: Cold Spring Harbor Laboratory Press). The choice of the regulatory elements constituting the chimeric gene depends essentially on the host species in which they must function, and those skilled in the art are capable of selecting regulatory elements which are functional in a given host organism. The term “functional” is intended to mean capable of functioning in a given host organism.

[0017] The promoters which the chimeric gene according to the invention can contain are either constitutive or inducible. A constitutive promoter according to the present invention is a promoter which induces the expression of a coding sequence in all the tissues of a host organism and continuously, i.e. throughout the duration of the life cycle of said organism. Some of these promoters may be tissue-specific, i.e. express the coding sequence continuously, but only in a particular tissue of the host organism. Constitutive promoters may originate from any type of organism. Among the constitutive promoters which can be used in the chimeric gene of the present invention, mention may, for example, be made of bacterial promoters, such as that of the octopine synthase gene or that of the nopaline synthase gene, of viral promoters, such as that of the gene controlling transcription of the 19S or 35S RNAs of the cauliflower mosaic virus (Odell et al., 1985, Nature, 313, 810-812), or the promoters of the cassava vein mosaic virus (as described in patent application WO 97/48819). Among the promoters of plant origin, mention will be made of the promoter of the ribulose-biscarboxylase/oxygenase (RuBisCO) small sub-unit gene, the promoter of a histone gene as described in application EP 0 507 698, or the promoter of a rice actin gene (U.S. Pat. No. 5,641,876).

[0018] According to another particular embodiment of the invention, the chimeric gene contains an inducible promoter. An inducible promoter is a promoter which only functions, i.e. which only induces expression of a coding sequence, when it is itself induced by an inducing agent. This inducing agent is generally a substance which can be synthesized in the host organism subsequent to a stimulus external to said organism, this external stimulus possibly being, for example, a pathogenic agent. The inducing agent may also be a substance external to this host organism, capable of penetrating into this host organism. Advantageously, the promoter used in the present invention is inducible subsequent to an attack on the host organism by a pathogenic agent. Such promoters are known, such as, for example, the promoter of the plant O-methyl-transferase class II (COMT II) gene described in patent application FR 99 03700, the Arabidopsis PR-1 promoter (Lebel et al., 1998, Plant J. 16(2):223-233), the EAS4 promoter of the tobacco sesquiterpene synthase gene (Yin et al., 1997, Plant Physiol. 115(2): 437-451), or the promoter of the gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase (Nelson et al., 1994, Plant Mol. Biol. 25(3): 401-412).

[0019] Among the terminator elements which may be used in the chimeric gene of the present invention, mention may, for example, be made of the nos terminator element of the gene encoding Agrobacterium tumefaciens nopaline synthase (Beven et al., 1983, Nucleic Acids Res. 11(2), 369-385), or the terminator element of a histone gene as described in application EP 0 633 317.

[0020] It also appears to be important for the chimeric gene to additionally comprise a signal peptide or a transit peptide which makes it possible to control and orient the production of the arogenate dehydrogenase enzyme specifically in a part of the host organism, such as, for example, the cytoplasm, a particular compartment of the cytoplasm, or the cell membrane or, in the case of plants, in a particular type of cellular compartment, for example the chloroplasts, or in the extracellular matrix.

[0021] The transit peptides can be either single or double. The double transit peptides are optionally separated by an intermediate sequence, i.e. they comprise, in the direction of transcription, a sequence encoding a transit peptide of a plant gene encoding an enzyme located in plastids, a portion of sequence of the mature N-terminal portion of a plant gene encoding an enzyme located in plastids, and then a sequence encoding a second transit peptide of a plant gene encoding an enzyme located in plastids. Such double transit peptides are, for example, described in patent application EP 0 508 909.

[0022] Signal peptides of use according to the invention which may be mentioned include in particular the signal peptide of the tobacco PR-1α gene described by Cornelissen et al. (1987, Nucleic Acid Res. 15, 6799-6811), in particular when the chimeric gene according to the invention is introduced into plant cells or plants, or the signal peptide of the Mat α1 factor precursor (Brake et al., 1985, In: Gething M.-J. (eds.); Protein transport and secretion, pp. 103-108, Cold Spring Harbor Laboratory Press, New York), when the chimeric gene according to the invention is introduced into yeast.

[0023] The present invention also relates to a vector containing a chimeric gene according to the invention. The vector according to the invention is of use for transforming a host organism and expressing an arogenate dehydrogenase enzyme in this host organism. This vector may be a plasmid, a cosmid, a bacteriophage or a virus. In general, the main qualities of this vector should be an ability to persist and to self-replicate in the host organism's cells, in particular by virtue of the presence of an origin of replication, and to express therein an arogenate dehydrogenase enzyme. The choice of such a vector and also the techniques for inserting the chimeric gene according to the invention therein are widely described in Sambrook et al. (1989, Molecular Cloning: A Laboratory Manual, Nolan C. ed., New York: Cold Spring Harbor Laboratory Press) and are part of the general knowledge of those skilled in the art. Advantageously, the vector used in the present invention also contains, in addition to the chimeric gene of the invention, a gene encoding a selectable marker. This selectable marker makes it possible to select the host organisms effectively transformed, i.e. those having incorporated the vector. According to a particular embodiment of the invention, the host organism to be transformed is a microorganism, in particular a yeast, a bacterium, a fungus or a virus. According to another embodiment, the host organism is a plant or a plant cell. Among the genes encoding selectable markers which can be used, mention may be made of genes for resistance to antibiotics, such as, for example, the hygromycin phosphotransferase (Gritz et al., 1983, Gene 25: 179-188), but also the genes for tolerance to herbicides, such as the bar gene (White et al., NAR 18: 1062, 1990) for tolerance to bialaphos, the EPSPS gene (U.S. Pat. No. 5,188,642) for tolerance to glyphosate or else the HPPD gene (WO 96/38567) for tolerance to isoxazoles. Mention may also be made of genes encoding readily identifiable enzymes such as the GUS enzyme, or genes encoding pigments or enzymes which regulate the production of pigments in the transformed cells. Such selectable marker genes are in particular described in patent applications WO 91/02071, WO 95/06128, WO 96/38567 and WO 97/04103.

[0024] The present invention also relates to transformed host organisms containing a vector as described above. The term “host organism” is intended to mean any lower or higher monocellular or pluricellular organism into which the chimeric gene according to the invention can be introduced, so as to produce arogenate dehydrogenase enzyme. They are in particular bacteria, for example Escherichia coli, yeast, in particular of the Saccharomyces, Kluyveromyces or Pichia genera, fungi, in particular Aspergillus, a baculovirus, or preferably plant cells and plants.

[0025] According to the invention, the term “plant cell” is intended to mean any cell derived from a plant and able to constitute undifferentiated tissues such as calluses, differentiated tissues such as embryos, parts of plants, plants or seeds.

[0026] According to the invention, the term “plant” is intended to mean any differentiated multicellular organism capable of photosynthesis, in particular monocotyledons or dicotyledons.

[0027] The term “transformed host organism” is intended to mean a host organism which has incorporated into its genome the chimeric gene of the invention and consequently produces an arogenate dehydrogenase enzyme in its tissues, or in a culture medium. Those skilled in the art can use one of the many known methods of transformation to obtain the host organisms according to the invention.

[0028] One of these methods consists in bringing the cells to be transformed into contact with polyethylene glycol (PEG) and the vectors of the invention (Chang and Cohen, 1979, Mol. Gen. Genet. 168(1), 111-115); Mercenier and Chassy, 1988, Biochimie 70(4), 503-517). Electroporation is another method, which consists in subjecting the cells or tissues to be transformed and the vectors of the invention to an electric field (Andreason and Evans, 1988, Biotechniques 6(7), 650-660; Shigekawa and Dower, 1989, Aust. J. Biotechnol. 3(1), 56-62). Another method consists in directly injecting the vectors into the host cells or tissues by microinjection (Gordon and Ruddle, 1985, Gene 33(2), 121-136). Advantageously, the “biolistic” method may be used. In consists in bombarding cells or tissues with particles onto which the vectors of the invention are adsorbed (Bruce et al., 1989, Proc. Natl. Acad. Sci. USA 86(24), 9692-9697; Klein et al., 1992, Biotechnology 10(3), 286-291; U.S. Pat. No. 4,945,050). Preferentially, the plant transformation will be carried out using bacteria of the Agrobacterium genus, preferably by infecting the cells or tissue of said plants by A. tumefaciens (Knopf, 1979, Subcell. Biochem. 6, 143-173; Shaw et al., 1983, Gene 23(3): 315-330) or A. rhizogenes (Bevan and Chilton, 1982, Annu. Rev. Genet. 16: 357-384; Tepfer and Casse-Delbart, 1987, Microbiol. Sci. 4(1), 24-28). Preferentially, the transformation of plant cells with Agrobacterium tumefaciens is carried out according to the protocol described by Ishida et al. (1996, Nat. Biotechnol. 14(6), 745-750).

[0029] Those skilled in the art will choose the appropriate method as a function of the nature of the host organism to be transformed.

[0030] The present invention therefore also relates to a method for preparing the arogenate dehydrogenase enzyme, comprising the steps of culturing a transformed host organism comprising a gene encoding an arogenate dehydrogenase enzyme as defined above, in a suitable culture medium, recovering the arogenate dehydrogenase enzyme produced from the culture medium by centrifugation or by filtration, and then purifying the recovered enzyme by passing it through at least one chromatography column. These steps bring about the extraction and the purification, which may be total or partial, of the arogenate dehydrogenase enzyme obtained. Preferentially, the transformed organism is a microorganism, in particular a bacterium, a yeast, a fungus or a virus.

[0031] The present invention also comprises a method for identifying a herbicidal compound having as a target an arogenate dehydrogenase enzyme, characterized in that:

[0032] (a) at least two samples, each containing an equivalent amount of arogenate dehydrogenase enzymes in solution, are prepared;

[0033] (b) one of the samples is treated with a compound;

[0034] (c) the arogenate dehydrogenase activity is measured in each one of said samples;

[0035] (d) the compound used in step (b) is identified as being a herbicidal compound when the activity measured in step (c) is significantly less in the treated sample compared to the untreated sample;

[0036] (e) the herbicidal activity of the compound identified in step (d) is validated by treating plants with said compound.

[0037] According to the present method, the measurement of the arogenate dehydrogenase activity is carried out by any method which makes it possible either to measure a decrease in the amount of arogenate substrate, or to measure an accumulation of a product derived from the enzyme reaction, namely L-tyrosine or the cofactor NADPH. In particular, the measurement of the arogenate dehydrogenase activity can be carried out by the method described in example 4. In addition, the herbicidal activity validated in step (e) of the present method may be a lethal activity resulting in the death of the treated plant, or an activity which significantly slows down the growth of the treated plant.

[0038] According to the invention, the term “compound” is intended to mean any chemical compound or mixture of chemical compounds, including peptides and proteins. According to the invention, the term “mixture of compounds” is understood to mean at least two different compounds, such as, for example, the (dia)stereoisomers of a molecule, mixtures of natural origin derived from the extraction of biological material (plants, plant tissues, bacterial cultures, yeast cultures or fungal cultures, insects, animal tissues, etc.) or unpurified or totally or partially purified reaction mixtures, or else mixtures of products derived from combinatorial chemistry techniques.

[0039] According to a particular embodiment of the method according to the invention, the arogenate dehydrogenase enzymes used originate from plants, preferably from Arabidopsis thaliana.

[0040] According to another embodiment of the method according to the invention, the arogenate dehydrogenase enzymes used originate from bacteria, preferably bacteria of the Synechocystis genus.

[0041] Preferably, the arogenate dehydrogenase enzymes used in the method according to the invention are the enzymes according to the present invention, in particular those represented by SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11 or SEQ ID NO: 13.

[0042] The invention also extends to the herbicidal compounds identified using the method mentioned above, in particular the herbicidal compounds having as a target an arogenate dehydrogenase enzyme, i.e. those which inhibit the activity of this enzyme. Preferentially, the herbicidal compounds are not general enzyme inhibitors. Also preferentially, the herbicidal compounds according to the invention are not compounds already known to have herbicidal activity.

[0043] The present invention also relates to herbicidal agrochemical compositions comprising, as active material, at least an effective amount of a herbicidal compound according to the invention.

[0044] According to the invention, the term “herbicidal agrochemical composition” is intended to mean a composition which can be applied preventatively or curatively to the areas on which cultivated plants are being or must be grown, in order to prevent the development of undesirable plants or “weeds” on the areas on which said cultivated plants are grown, whatever their state of development. An effective amount of herbicidal compound according to the invention corresponds to an amount of compound which makes it possible to destroy or inhibit the growth of the undesirable plants.

[0045] The herbicidal agrochemical compositions according to the invention comprise a herbicidal compound according to the invention or one of its agriculturally acceptable salts or a metal or metalloid complex of this compound, in combination with an agriculturally acceptable solid or liquid carrier and/or a surfactant, also agriculturally acceptable. In particular, the usual inert carriers and the usual surfactants can be used. These compositions cover not only the compositions ready to be applied to a plant or a seed to be treated using a suitable device, such as a spraying or dusting device, but also the concentrated commercially available compositions which must be diluted before they are applied to the crop.

[0046] The herbicidal compositions according to the invention may also contain many other ingredients, such as, for example, protective colloids, adhesives, thickeners, thixotropic agents, penetrating agents, stabilizers or sequestering agents. More generally, the active materials can be combined with any solid or liquid additives which comply with the usual formulating techniques.

[0047] According to the present invention, the term “carrier” denotes a natural or synthetic, organic or inorganic material with which the active material is combined in order to facilitate its application to the parts of the plant. This carrier is therefore generally inert and it must be agriculturally acceptable. The carrier may be solid (for example clays, natural or synthetic silicates, silica, resins, waxes, solid fertilizers) or liquid (for example water, alcohols, in particular butanol).

[0048] The surfactant may be an emulsifier, dispersing agent or wetting agent of the ionic or nonionic type, or a mixture of such surfactants. Mention may, for example, be made of polyacrylic acid salts, lignosulfonic acid salts, phenolsulfonic or naphthalenesulfonic acid salts, polycondensates of ethylene oxide with fatty alcohols or with fatty acids or with fatty amines, substituted phenols (in particular alkylphenols or arylphenols), salts of sulfosuccinic acid esters, taurine derivatives (in particular alkyl taurates), phosphoric esters of alcohols or of phenols which are polyoxyethylated, esters of fatty acids and of polyols, and derivatives of the above compounds containing sulfate, sulfonate and phosphate functions. The presence of at least one surfactant is generally essential when the active material and/or the inert carrier are not water-soluble and when the vector agent for the application is water.

[0049] The present invention also relates to transgenic plants tolerant to a herbicidal compound having as a target an enzyme involved in one of the metabolic steps of conversion of prephenate to L-tyrosine, characterized in that they contain a gene encoding a prephenate dehydrogenase enzyme and express said enzyme in their tissue. A prephenate dehydrogenase enzyme is an enzyme which catalyzes the reaction of conversion of prephenate to p-hydroxyphenylpyruvate. The identification of an enzyme with prephenate dehydrogenase activity can be carried out by any method which makes it possible either to measure a decrease in the amount of the prephenate substrate, or to measure an accumulation of a product derived from the enzyme reaction, namely p-hydroxyphenylpyruvate or one of the cofactors NADH or NADPH. In particular, the measurement of the prephenate dehydrogenase activity can be carried out using the method described in example 4.

[0050] According to a particular embodiment of the invention, the transgenic plants according to the invention are tolerant with respect to a herbicidal compound having as a target an arogenate dehydrogenase enzyme, preferably an arogenate dehydrogenase enzyme as described in the present invention.

[0051] According to another particular embodiment of the invention, the transgenic plants according to the invention are tolerant with respect to a herbicidal compound having as a target a prephenate aminotransferase enzyme.

[0052] According to a particular embodiment of the invention, the gene encoding the prephenate dehydrogenase enzyme expressed in the tolerant plants according to the invention is a yeast gene. Preferably, it is the gene encoding the Saccharomyces cerevisiae prephenate dehydrogenase enzyme (accession No. NC001134) as described in Mannhaupt et al. (1989, Gene 85, 303-311) and represented by the sequence identifier SEQ ID NO: 14.

[0053] According to another particular embodiment of the invention, the gene encoding the prephenate dehydrogenase enzyme expressed in the tolerant plants according to the invention is a bacterial gene. Preferably, it is a gene from a bacterium of the Bacillus genus, in particular of the species B. subtilis (accession No. M80245) as represented by the sequence identifier SEQ ID NO: 16. Preferably, it is a gene from a bacterium of the Escherichia genus, in particular of the species E. coli (accession No. M10431) as described in Hudson et al. (1984, J. Mol. Biol. 180(4), 1023-1051) and represented by the sequence identifier SEQ ID NO: 18. Preferably, it is a gene from a bacterium of the Erwinia genus, in particular the species E. herbicola (accession No. 43343) as represented by the sequence identifier SEQ ID NO: 20.

[0054] According to particular embodiment of the invention, the gene encoding the prephenate dehydrogenase enzyme expressed in the tolerant plants according to the invention is a fungal gene.

[0055] The transgenic plants according to the invention are obtained by genetic transformation with a gene encoding a prephenate dehydrogenase enzyme. Preferably, this gene is a chimeric gene comprising, functionally linked to one another, at least one promoter which is functional in a host organism, a polynucleotide encoding a prephenate dehydrogenase enzyme, and a terminator element which is functional in this same host organism. This gene is generally introduced into a vector, which is used to introduce said gene into said plants by one of the methods of transformation described above.

[0056] The present invention also relates to a method for producing plants tolerant with respect to herbicidal compounds having as a target an enzyme involved in one of the metabolic steps for conversion of prephenate to L-tyrosine, characterized in that said plants are transformed with a gene encoding a prephenate dehydrogenase enzyme in such a way that they express it in their tissues.

[0057] According to a particular embodiment of the invention, the present method applies to the production of plants tolerant with respect to a herbicidal compound having as a target an arogenate dehydrogenase enzyme as described in the present invention.

[0058] According to another particular embodiment of the invention, the present method applies to the production of plants tolerant with respect to a herbicidal compound having as a target a prephenate aminotransferase enzyme.

[0059] The present method therefore also comprises a method for producing plants tolerant with respect to a herbicidal compound having as a target an arogenate dehydrogenase enzyme, characterized in that said plants are transformed with a gene encoding a prephenate dehydrogenase enzyme in such a way that they express it in their tissues.

[0060] The transgenic plants according to the invention may also contain, in addition to a gene encoding a prephenate dehydrogenase enzyme, at least one other gene containing a polynucleotide encoding a protein of interest. Among these polynucleotides encoding a protein of interest, mention may be made of polynucleotides encoding an enzyme for resistance to a herbicide, for example the polynucleotide encoding the bar enzyme (White et al., NAR 18:1062, 1990) for tolerance to bialaphos, the polynucleotide encoding the EPSPS enzyme (U.S. Pat. No. 5,188,642; WO 97/04103) for tolerance to glyphosate, or else the polynucleotide encoding the HPPD enzyme (WO 96/38567) for tolerance to isoxazoles. Mention may also be made of a polynucleotide encoding an insecticidal toxin, for example a polynucleotide encoding a toxin of bacterium Bacillus thuringiensis (for example, see International Patent Application WO 98/40490). Other polynucleotides for resistance to diseases may also be contained in these plants, for example a polynucleotide encoding the oxaylate oxidase enzyme as described in patent application EP 0 531 498 or U.S. Pat. No. 5,866,778, or a polynucleotide encoding another antibacterial and/or antifungal peptide, such as those described in patent applications WO 97/30082, WO 99/24594, WO 99/02717, WO 99/53053 and WO 99/91089. Mention may also be made of polynucleotides encoding agronomic characteristics of the plant, in particular a polynucleotide encoding a delta-6 desaturase enzyme, as described in U.S. Pat. Nos. 5,552,306 and 5,614,313, and patent applications WO 98/46763 and WO 98/46764, or a polynucleotide encoding a serine acetyltransferase (SAT) enzyme, as described in patent applications WO 00/01833 and PCT/FR 99/03179.

[0061] The following examples make it possible to illustrate the present invention without, however, limiting the scope thereof.

EXAMPLE 1 Identification of the Gene Encoding the Arabidopsis Thaliana Arogenate Dehydrogense Enzyme

[0062] A comparison of the sequences of all the prephenate dehydrogenase and arogenate dehydrogenase enzymes currently available in the public databases (http://www/ncbi/nlm/nih/gov) revealed four short portions of homologous sequences. The enzymes compared are yeast prephenate dehydrogenase (accession number: Z36065), Bacillus subtilis prephenate dehydrogenase (accession number: M80245) and Synechocystis prephenate dehydrogenase (accession number: D90910). These portions of homology made it possible to identify an A. thaliana gene (accession number: AF096371) initially noted as encoding an enzyme “similar to the specific D-isomer 2-hydroxy acid dehydrogenase”. This gene consists of two exons separated by a 94 bp intron. The first exon comprises a 1.08 kb open reading frame containing a putative chloroplast transit peptide sequence located downstream of the first ATG codon. The second exon potentially encodes an 892 bp open reading frame. A very strong homology of approximately 60% exists between the protein sequences deduced from the two exons. This homology extends to 70% if the putative chloroplast transit peptide sequence located in the first exon is not taken into account. In addition, each one of the two predicted protein sequences has the size and possesses the four homologous portions characteristic of the prephenate/arogenate dehydrogenase enzymes. This gene was named TyrA (SEQ ID NO: 1).

EXAMPLE 2 Transcriptional Characterization of TyrA

[0063] The size of the transcript of the TyrA gene was determined using the Northern blotting and PCR techniques. Purified mRNAs extracted from young leaves of A. thaliana were hybridized with ³²P-radiolabeled probes corresponding to fragments of DNA of the two exons of TyrA. This analysis made it possible to identify a 1.8-1.9 kb transcript very close to the presumed size of an mRNA containing the two exons. In addition, although the complete cDNA could not be amplified by PCR, a 1.5 kb PCR fragment was obtained. This fragment comprises the 5′ oligonucleotide (P8=5′-GCTAAAACTCTTCTCCTTCAATACTTACCTG-3′) beginning at position 513 bp, and the 3′ oligonucleotide (P7=5′-CAGTATAATTAGTAGTCAAGGATCCTGACTGAGAG-3′) complementary to the 3'UTR and beginning at position 2053 bp. This fragment contains a portion of the first coding sequence (TyrA-At1) and the complete sequence of the second coding sequence (TyrA-AT2). Analysis of the sequence of this cDNA confirmed the splicing of the intron. The results of the analyses by Northern blotting and PCR strongly suggests the existence of an mRNA transcript containing the two coding regions TyrA-At1 (SEQ ID NO: 4) and TyrA-AT2 (SEQ ID NO: 6).

EXAMPLE 3 Preparation of Constructs Containing the Various Coding Sequences of the A. Thaliana Arogenate Dehydrogenase

[0064] The first exon TyrA-At1 was obtained by PCR amplification of the genomic DNA of A. thaliana with the oligonucleotide P1 (5′-TCTCCATATGATCTTTCAATCTCAT-TCTCATC-3′) which introduces an Nde I restriction site (underlined) at the first ATG codon, and the oligonucleotide P2 (5′-CTAACTAACTAACTACATA-CCTCATCATATCC-3′) which is complementary to the 3′ end of the first exon and to the 5′ end of the intron and introduces a stop codon (underlined). Three constructs lacking the sequence encoding the transit peptide were also produced with the oligonucleotide P3 (5′-CCTCTCTTTCCATATGCTCCCTTCTC-3′) which introduces an Nde I restriction site (underlined) at the second ATG codon (M43) at position 127, the oligonucleotide P4 (5′-CCGCCAGCCACCTCCATATGACCGACACCATCC-3′) which introduces an ATG initiating codon and an Nde I restriction site (underlined) at position 174 from the first ATG codon (V58M), and the oligonucleotide P5 (5′-CGCCACCCCTCATATGCGTATCGCC-3′) which introduces an ATG initiating codon and an Nde I restriction site (underlined) at position 222 from the first ATG codon (L75M). All the OCR fragments corresponding to the first exon, which may or may not encode a transit peptide, were cloned into the plasmid pPCR-Script (Stratagene). Nde I-BamH I DNA fragments containing the coding sequences, with or without the transit peptide sequence, were then cloned into the plasmid pET21 a(+) (Novagen), leading to the development of the plasmids pET21-TyrA-AT1, with and without transit peptide sequence (pET21-TyrA-AT1-M1,pET21-TyrA-AT1-M43, pET21-TyrA-ATI-M58 and pET21-TyrA-ATi-M75).

[0065] Two other oligonucleotides were used to amplify the second coding sequence (TyrA-AT2). The oligonucleotide P6 (5′-GATGCATCTTTGCATATGATGAGGTCAGAAGATG-3′) introduces an Nde I restriction site (underlined) at the ATG codon of the second open reading frame (at position 1081 from the first ATG codon), and the oligonucleotide P7 (5′-CAGTATAATTAGTAGTCAAGGATCCTGACTGAGAG-3′), complementary to the start of the 3′-UTR, introduces a BamH I restriction site (underlined). The PCR fragment corresponding to the second coding sequence was digested with Nde I-BamH I and then cloned into the plasmid pET21 a(+), giving the plasmid pET21-TyrA-AT2.

[0066] The complete coding sequence was reconstituted by assembly of the missing 5′ end of the first exon with a partial TyrA-AT cDNA (1.5 kb), obtained by PCR amplification of the Arabidopsis cDNA with the oligonucleotide P8 (5′-GCTAAAACTCTTCTCCTTCAATACTTACCTG-3′) beginning at position 513 bp from the first ATG codon, and the 3′ oligonucleotide P7. An EcoRV restriction site located at position 812 bp from the first ATG codon and present in the 5′ end of the partial TyrA-AT cDNA was used for the reconstitution. The partial TyrA-AT cDNA was cloned into the plasmid pPCR-Script. An EcoRV-EcoRV fragment was obtained from the plasmid pPCR-Script-TyrA-AT and then cloned into the plasmid pPCR-Script-TyrA-AT1 digested beforehand with EcoRV. This manipulation led to the plasmid pPCR-Script-TyrA-ATc being obtained. An Nde1-BamH1 fragment containing the complete coding sequence was excised from the plasmid pPCR-Script-TyrA-ATc, and then cloned into a plasmid pET21a(+) (Novagen), digested beforehand with Nde1 and BamH1, producing the plasmid pET2la(+)-TyrA-ATc. Then, in the same way as for the first exon, four plasmids pET21a(+)-TyrA-ATc were obtained; a plasmid containing the complete coding sequence with the sequence encoding the putative transit peptide, and three plasmids lacking this transit peptide sequence, which was cleaved at three different sites (M43, V58 and L75, see above).

[0067] For all the constructs described above, the cDNA inserts were sequenced in order to be sure that no unwanted mutation had been introduced during the PCR amplification.

EXAMPLE 4 Measurement of the Enzyme Activities

[0068] The arogenate dehydrogenase activity is measured at 25° C. by spectrophotometric monitoring, at 340 nm, of the formation of NADH or NADPH in a solution containing 50 mM of Tris-HCl, pH 8.6, 300 μm of arogenate and 1 mM of NAD or NADPH in a total volume of 200 μl.

[0069] The prephenate dehydrogenase activity is measured at 25° C. by spectrophotometric monitoring, at 340 nm, of the formation of NADH or NADPH in a solution containing 50 mM of Tris-HCl, pH 8.6, 300 μM of prephenate and 1 mM of NAD or NADPH in a total volume of 200 μl.

EXAMPLE 5 Production of Recombinant Arogenate Dehydrogenase

[0070]Eshcerichia coli AT2471 cells were transformed with each one of the plasmids pET21-TyrA-AT obtained in example 3, and then cultured at 37° C. in 2 liters of Luria-Bertani medium supplemented with 100 μg/ml of carbenicillin. When the culture had reached the equivalent of an absorbance at 600 nm (A600) of 0.6, 1 mM of isopropyl-β-D-thiogalactoside was added to the culture medium in order to induce recombinant protein synthesis. The cells were then cultured for 16 h at 28° C., harvested, and then centrifuged for 20 min at 40 000 g. The pellet was then resuspended in a 50 mM Tris-HCl buffer, pH 7.5, containing 1 mM EDTA, 1 mM dithiothreitol, 1 mM benzamidine HCl and 5 mM aminocaproic acid, and then sonicated (100 pulses every 3 seconds at power 5) with a Vibra-Cell disrupter (Sonics and Materials, Danbury, Conn., USA). The crude extracts thus obtained were then centrifuged for 20 min at 40 000 g, and the supernatants were used directly for the enzyme assays.

[0071] The SDS-PAGE analyses of total protein extracts of the E. coli strain AT 2471 containing the various constructs pET21-TyrA-Atc, pET21-TyrA-AT1 and pET21-TyrA-AT2 revealed the presence of three recombinant proteins having molecular masses of 66-68 kDa, 35 kDa and 33-34 kDa, respectively. These molecular masses correspond well to the masses deduced from their respective coding sequences (68786 Da for TyrA-ATc, 34966 Da for Tyr-A-AT1, and 34069 Da for Tyr-A-AT2). For the transformants containing the complete coding sequence (TyrA-Atc) and the first coding sequence (TyrA-AT1), recombinant proteins were observed only with the constructs encoding the proteins M58-TyrA-Atc and M58-TyrA-AT1. The three recombinant proteins were mainly found in the protein bodies. However, the presence of small amounts of recombinant proteins in the soluble protein extracts of E. coli made it possible to characterize the biochemical properties.

EXAMPLE 6 Identification and Biochemical Characterization of the Arabidopsis Thaliana Arogenate Dehydrogenase Enzymes

[0072] The biochemical characterization of the recombinant arogenate dehydrogenase enzymes was carried out using the soluble protein extracts of the transformed E. coli strains. The arogenate dehydrogenase activity was measured according to the method described in example 4. A strictly NADP-dependent arogenate dehydrogenase activity was demonstrated for each one of the three recombinant enzymes. No arogenate dehydrogenase activity was detected in the presence of NAD, and no prephenate dehydrogenase activity was detected whatever the cofactor used (NADP or NAD) and whatever the protein tested (TyrA-ATc, TyrA-AT1 or TyrA-AT2). In addition, prephenate at a concentration of 1 mM does not inhibit the arogenate dehydrogenase activity of the three recombinant enzymes. Each one of these enzymes has a Michaelis-Menten-type behavior, and their Km value for arogenate and NADP is relatively the same (FIGS. 2 and 3). The Michaelis constants for NADP are, respectively, 40 μM for TyrA-Atc, 60 μM for TyrA-AT1, and 20 μM for TyrA-AT2. The Michaelis constants for arogenate are, respectively, 70 μM for TyrA-Atc, 45 μM for TyrA-AT1, and 45 μM for TyrA-AT2. In addition, like the other plant arogenate dehydrogenases (Byng et al., 1981, Phytochemistry 6, 1289-1292; Connelly and Conn, 1986, Z. Naturforsch 41c, 69-78; Gaines et al., 1982 Planta 156, 233-240), the Arabidopsis arogenate dehydrogenases are all very sensitive to tyrosine, the product of the enzyme reaction, and insensitive to 1 mM of phenylalanine and 1 mM of p-hydroxyphenylpyruvate. The inhibition by tyrosine is competitive with respect to arogenate (Ki of 14 μM for TyrA-Atc, 8 μM for TyrA-AT1, and 12 μM for TyrA-AT2), and noncompetitive with respect to NADP.

EXAMPLE 7 Identification and Biochemical Characterization of the Syfnechocystis Arogenate Dehydrogenase Enzyme

[0073] The sequence of the gene encoding the A. thaliana arogenate dehyrogenase identified in example 1 (TyrA) made it possible to identify an arogenate dehydrogenase gene in the bacterium Synechocystis (accession number: 1652956). This gene was originally described as encoding a “prephenate dehydrogenase” enzyme. It was isolated from a Synechocystis genomic library and the enzyme was produced in the same way as the A. thaliana enzyme, according to the protocol described in example 5. Biochemical characterization of the enzyme produced made it possible to demonstrate that it is an arogenate dehydrogenase enzyme and not a prephenate dehydrogenase enzyme. This biochemical characterization of the Synechocystis arogenate dehydrogenase enzyme was carried out using the purified soluble protein extracts of the transformed E. coli strains. The arogenate dehydrogenase activity was measured according to the method described in example 4. A strictly NADP-dependent arogenate dehydrogenase activity was demonstrated for this enzyme. No arogenate dehydrogenase activity was detected in the presence of NAD, and no prephenate dehydrogenase activity was detected whatever the cofactor used (NADP or NAD). In addition, prephenate at a concentration of 1 mM does not inhibit the arogenate dehydrogenase activity of this enzyme. The Synechocystis arogenate dehydrogenase has a Michaelis-Menten-type behavior (FIG. 4). The Michaelis constant is 6 μM for NADP, and 107 μM for arogenate.

EXAMPLE 8 Identification of Other Plant Arogenate Dehydrogenase Enzymes

[0074] The sequence of the gene encoding the A. thaliana arogenate dehydrogenase identified in example 1 (TyrA) made it possible to identify another arogenate dehydrogenase gene in A. thaliana. This new gene (accession number: AC0342561; SEQ ID NO: 8) was initially noted as “containing similarity with the embryo abundance protein (EMB20) of Picea glauca”. It also has a putative chloroplast transit peptide sequence, but no repeat region.

[0075] The sequence of the TyrA gene also made it possible to identify two other cDNAs encoding arogenate dehydrogenase enzymes in the public EST (Expressed Sequence Tags) databases. One of these cDNAs, which is not complete, corresponds to a tomato cDNA (TC41067; SEQ ID NO: 22). The incomplete nature of this cDNA does not make it possible to determine whether it is duplicated like TyrA, since its 3′ end stops just after the codon corresponding to D356 of Tyr-AT1. The second cDNA corresponds to a complete cDNA of Picea glauca (accession number: L47749; SEQ ID NO: 10) and does not possess a repeat region. This Picea glauca cDNA was noted as being an “embryo abundance protein”.

1 30 1 2082 DNA Arabidopsis thaliana transit_peptide (1)..(174) Intron (1089)..(1181) 1 atgatctttc aatctcattc tcatcatctt cttctctatc aatcctcatc ttcctcctcc 60 ttcttcttcc tcccaaagct catcaccaaa cctcctctct ccctctcatt tacctctctt 120 tcctcaatgc tcccttctct ctctctctcc accgccaacc gccacctctc cgtcaccgac 180 accatccctc ttcccaactc caactccaac gccacccctc ctctccgtat cgccatcatc 240 ggattcggaa actacggcca attccttgcc gaaaccctaa tttctcaagg ccacattctc 300 ttcgctcact cccgatccga tcactcctcc gccgctcgcc gtctcggtgt ctcatacttc 360 accgatcttc acgatctctg cgaacgtcat cctgacgtag tccttctctg tacttcaatc 420 ctctccatag agaatattct caaaacgttg ccgtttcaga gactccgtcg caacactctc 480 ttcgttgatg ttctctccgt taaagagttt gctaaaactc ttctccttca atacttacct 540 gaagatttcg atattctttg tacacatcca atgtttggtc ctcagagtgt gagttcaaat 600 catggctgga gaggattaag atttgtgtat gataaagtta ggattgggga agagagattg 660 agagtctcaa ggtgtgagag ttttcttgag atttttgtta gagaaggatg tgagatggtg 720 gagatgagtg ttactgatca tgataagttt gctgctgaat cacagtttat aactcatact 780 cttggtaggc ttttggggat gttgaagttg atatcgacgc cgattaatac gaaagggtac 840 gaggcgttgc ttgatttagc tgagaatatt tgtggggata gttttgattt gtattatggg 900 ttgtttgtgt ataataacaa ctctttggag gtgttagaga ggattgattt ggctttcgag 960 gctttgcgta aggagctttt tagtcggctt cacggtgttg tgaggaagca gtcttttgaa 1020 ggtgaagcaa agaaagttca tgtttttcca aattgtggtg aaaatgatgc ttctttggat 1080 atgatgaggt atgtagttag ttagttagtt acattgtgtg gtttgatgca ttttggattt 1140 ggtttcttat tgtaaatagt tatcgatttg tgatcttgca ggtcagaaga tgttgttgtg 1200 aagtatgaat ataactccca ggtgtctggt agtgttaatg acggttcgag gctcaagatt 1260 ggtatcgtcg ggtttggaaa ttttggacag tttctaggta aaaccatggt caagcagggt 1320 cacactgtgt tagcttattc cagaagtgac tacactgatg aagcagcaaa gctcggtgtt 1380 tcgtattttt cagatcttga tgatctattt gaagagcatc ctgaagttat tattctctgt 1440 acgtcaatcc tttcgactga aaaagttctc gagtcactac cgtttcagag actgaagaga 1500 agcacacttt ttgtggatgt actctcagta aaagagttcc cgaggaattt atttcttcaa 1560 actctcccac aagattttga tattttgtgc acgcatccta tgtttgggcc agagagtggt 1620 aaaaatggat ggaacaatct tgcctttgtg tttgataagg ttaggattgg aatggatgat 1680 agaagaaaat cgaggtgtaa cagttttctt gatatttttg cccgtgaagg atgtcgtatg 1740 gtggagatgt cgtgtgctga acatgattgg catgctgctg gatcacagtt tatcacacac 1800 acagtgggaa ggcttctgga gaagctgagc ttggaatcta ctcctataga taccaaaggt 1860 tatgagacat tgctaaaact ggtggagaat actgctggtg acagctttga tctgtactat 1920 ggactatttt tatacaatcc taatgcaatg gaacagcttg agaggtttca tgtggctttt 1980 gaatcattga agacacagct ctttggacga ctacattctc aacattctca tgagctagct 2040 aaatcatctt ccccaaagac aactaagcta ttaactagct aa 2082 2 1981 DNA Arabidopsis thaliana CDS (1)..(1980) transit_peptide (1)..(174) 2 atg atc ttt caa tct cat tct cat cat ctt ctt ctc tat caa tcc tca 48 Met Ile Phe Gln Ser His Ser His His Leu Leu Leu Tyr Gln Ser Ser 1 5 10 15 tct tcc tcc tcc ttc ttc ttc ctc cca aag ctc atc acc aaa cct cct 96 Ser Ser Ser Ser Phe Phe Phe Leu Pro Lys Leu Ile Thr Lys Pro Pro 20 25 30 ctc tcc ctc tca ttt acc tct ctt tcc tca atg ctc cct tct ctc tct 144 Leu Ser Leu Ser Phe Thr Ser Leu Ser Ser Met Leu Pro Ser Leu Ser 35 40 45 ctc tcc acc gcc aac cgc cac ctc tcc gtc acc gac acc atc cct ctt 192 Leu Ser Thr Ala Asn Arg His Leu Ser Val Thr Asp Thr Ile Pro Leu 50 55 60 ccc aac tcc aac tcc aac gcc acc cct cct ctc cgt atc gcc atc atc 240 Pro Asn Ser Asn Ser Asn Ala Thr Pro Pro Leu Arg Ile Ala Ile Ile 65 70 75 80 gga ttc gga aac tac ggc caa ttc ctt gcc gaa acc cta att tct caa 288 Gly Phe Gly Asn Tyr Gly Gln Phe Leu Ala Glu Thr Leu Ile Ser Gln 85 90 95 ggc cac att ctc ttc gct cac tcc cga tcc gat cac tcc tcc gcc gct 336 Gly His Ile Leu Phe Ala His Ser Arg Ser Asp His Ser Ser Ala Ala 100 105 110 cgc cgt ctc ggt gtc tca tac ttc acc gat ctt cac gat ctc tgc gaa 384 Arg Arg Leu Gly Val Ser Tyr Phe Thr Asp Leu His Asp Leu Cys Glu 115 120 125 cgt cat cct gac gta gtc ctt ctc tgt act tca atc ctc tcc ata gag 432 Arg His Pro Asp Val Val Leu Leu Cys Thr Ser Ile Leu Ser Ile Glu 130 135 140 aat att ctc aaa acg ttg ccg ttt cag aga ctc cgt cgc aac act ctc 480 Asn Ile Leu Lys Thr Leu Pro Phe Gln Arg Leu Arg Arg Asn Thr Leu 145 150 155 160 ttc gtt gat gtt ctc tcc gtt aaa gag ttt gct aaa act ctt ctc ctt 528 Phe Val Asp Val Leu Ser Val Lys Glu Phe Ala Lys Thr Leu Leu Leu 165 170 175 caa tac tta cct gaa gat ttc gat att ctt tgt aca cat cca atg ttt 576 Gln Tyr Leu Pro Glu Asp Phe Asp Ile Leu Cys Thr His Pro Met Phe 180 185 190 ggt cct cag agt gtg agt tca aat cat ggc tgg aga gga tta aga ttt 624 Gly Pro Gln Ser Val Ser Ser Asn His Gly Trp Arg Gly Leu Arg Phe 195 200 205 gtg tat gat aaa gtt agg att ggg gaa gag aga ttg aga gtc tca agg 672 Val Tyr Asp Lys Val Arg Ile Gly Glu Glu Arg Leu Arg Val Ser Arg 210 215 220 tgt gag agt ttt ctt gag att ttt gtt aga gaa gga tgt gag atg gtg 720 Cys Glu Ser Phe Leu Glu Ile Phe Val Arg Glu Gly Cys Glu Met Val 225 230 235 240 gag atg agt gtt act gat cat gat aag ttt gct gct gaa tca cag ttt 768 Glu Met Ser Val Thr Asp His Asp Lys Phe Ala Ala Glu Ser Gln Phe 245 250 255 ata act cat act ctt ggt agg ctt ttg ggg atg ttg aag ttg ata tcg 816 Ile Thr His Thr Leu Gly Arg Leu Leu Gly Met Leu Lys Leu Ile Ser 260 265 270 acg ccg att aat acg aaa ggg tac gag gcg ttg ctt gat tta gct gag 864 Thr Pro Ile Asn Thr Lys Gly Tyr Glu Ala Leu Leu Asp Leu Ala Glu 275 280 285 aat att tgt ggg gat agt ttt gat ttg tat tat ggg ttg ttt gtg tat 912 Asn Ile Cys Gly Asp Ser Phe Asp Leu Tyr Tyr Gly Leu Phe Val Tyr 290 295 300 aat aac aac tct ttg gag gtg tta gag agg att gat ttg gct ttc gag 960 Asn Asn Asn Ser Leu Glu Val Leu Glu Arg Ile Asp Leu Ala Phe Glu 305 310 315 320 gct ttg cgt aag gag ctt ttt agt cgg ctt cac ggt gtt gtg agg aag 1008 Ala Leu Arg Lys Glu Leu Phe Ser Arg Leu His Gly Val Val Arg Lys 325 330 335 cag tct ttt gaa ggt gaa gca aag aaa gtt cat gtt ttt cca aat tgt 1056 Gln Ser Phe Glu Gly Glu Ala Lys Lys Val His Val Phe Pro Asn Cys 340 345 350 ggt gaa aat gat gct tct ttg gat atg atg agg tca gaa gat gtt gtt 1104 Gly Glu Asn Asp Ala Ser Leu Asp Met Met Arg Ser Glu Asp Val Val 355 360 365 gtg aag tat gaa tat aac tcc cag gtg tct ggt agt gtt aat gac ggt 1152 Val Lys Tyr Glu Tyr Asn Ser Gln Val Ser Gly Ser Val Asn Asp Gly 370 375 380 tcg agg ctc aag att ggt atc gtc ggg ttt gga aat ttt gga cag ttt 1200 Ser Arg Leu Lys Ile Gly Ile Val Gly Phe Gly Asn Phe Gly Gln Phe 385 390 395 400 cta ggt aaa acc atg gtc aag cag ggt cac act gtg tta gct tat tcc 1248 Leu Gly Lys Thr Met Val Lys Gln Gly His Thr Val Leu Ala Tyr Ser 405 410 415 aga agt gac tac act gat gaa gca gca aag ctc ggt gtt tcg tat ttt 1296 Arg Ser Asp Tyr Thr Asp Glu Ala Ala Lys Leu Gly Val Ser Tyr Phe 420 425 430 tca gat ctt gat gat cta ttt gaa gag cat cct gaa gtt att att ctc 1344 Ser Asp Leu Asp Asp Leu Phe Glu Glu His Pro Glu Val Ile Ile Leu 435 440 445 tgt acg tca atc ctt tcg act gaa aaa gtt ctc gag tca cta ccg ttt 1392 Cys Thr Ser Ile Leu Ser Thr Glu Lys Val Leu Glu Ser Leu Pro Phe 450 455 460 cag aga ctg aag aga agc aca ctt ttt gtg gat gta ctc tca gta aaa 1440 Gln Arg Leu Lys Arg Ser Thr Leu Phe Val Asp Val Leu Ser Val Lys 465 470 475 480 gag ttc ccg agg aat tta ttt ctt caa act ctc cca caa gat ttt gat 1488 Glu Phe Pro Arg Asn Leu Phe Leu Gln Thr Leu Pro Gln Asp Phe Asp 485 490 495 att ttg tgc acg cat cct atg ttt ggg cca gag agt ggt aaa aat gga 1536 Ile Leu Cys Thr His Pro Met Phe Gly Pro Glu Ser Gly Lys Asn Gly 500 505 510 tgg aac aat ctt gcc ttt gtg ttt gat aag gtt agg att gga atg gat 1584 Trp Asn Asn Leu Ala Phe Val Phe Asp Lys Val Arg Ile Gly Met Asp 515 520 525 gat aga aga aaa tcg agg tgt aac agt ttt ctt gat att ttt gcc cgt 1632 Asp Arg Arg Lys Ser Arg Cys Asn Ser Phe Leu Asp Ile Phe Ala Arg 530 535 540 gaa gga tgt cgt atg gtg gag atg tcg tgt gct gaa cat gat tgg cat 1680 Glu Gly Cys Arg Met Val Glu Met Ser Cys Ala Glu His Asp Trp His 545 550 555 560 gct gct gga tca cag ttt atc aca cac aca gtg gga agg ctt ctg gag 1728 Ala Ala Gly Ser Gln Phe Ile Thr His Thr Val Gly Arg Leu Leu Glu 565 570 575 aag ctg agc ttg gaa tct act cct ata gat acc aaa ggt tat gag aca 1776 Lys Leu Ser Leu Glu Ser Thr Pro Ile Asp Thr Lys Gly Tyr Glu Thr 580 585 590 ttg cta aaa ctg gtg gag aat act gct ggt gac agc ttt gat ctg tac 1824 Leu Leu Lys Leu Val Glu Asn Thr Ala Gly Asp Ser Phe Asp Leu Tyr 595 600 605 tat gga cta ttt tta tac aat cct aat gca atg gaa cag ctt gag agg 1872 Tyr Gly Leu Phe Leu Tyr Asn Pro Asn Ala Met Glu Gln Leu Glu Arg 610 615 620 ttt cat gtg gct ttt gaa tca ttg aag aca cag ctc ttt gga cga cta 1920 Phe His Val Ala Phe Glu Ser Leu Lys Thr Gln Leu Phe Gly Arg Leu 625 630 635 640 cat tct caa cat tct cat gag cta gct aaa tca tct tcc cca aag aca 1968 His Ser Gln His Ser His Glu Leu Ala Lys Ser Ser Ser Pro Lys Thr 645 650 655 act aag cta tta a 1981 Thr Lys Leu Leu 660 3 660 PRT Arabidopsis thaliana 3 Met Ile Phe Gln Ser His Ser His His Leu Leu Leu Tyr Gln Ser Ser 1 5 10 15 Ser Ser Ser Ser Phe Phe Phe Leu Pro Lys Leu Ile Thr Lys Pro Pro 20 25 30 Leu Ser Leu Ser Phe Thr Ser Leu Ser Ser Met Leu Pro Ser Leu Ser 35 40 45 Leu Ser Thr Ala Asn Arg His Leu Ser Val Thr Asp Thr Ile Pro Leu 50 55 60 Pro Asn Ser Asn Ser Asn Ala Thr Pro Pro Leu Arg Ile Ala Ile Ile 65 70 75 80 Gly Phe Gly Asn Tyr Gly Gln Phe Leu Ala Glu Thr Leu Ile Ser Gln 85 90 95 Gly His Ile Leu Phe Ala His Ser Arg Ser Asp His Ser Ser Ala Ala 100 105 110 Arg Arg Leu Gly Val Ser Tyr Phe Thr Asp Leu His Asp Leu Cys Glu 115 120 125 Arg His Pro Asp Val Val Leu Leu Cys Thr Ser Ile Leu Ser Ile Glu 130 135 140 Asn Ile Leu Lys Thr Leu Pro Phe Gln Arg Leu Arg Arg Asn Thr Leu 145 150 155 160 Phe Val Asp Val Leu Ser Val Lys Glu Phe Ala Lys Thr Leu Leu Leu 165 170 175 Gln Tyr Leu Pro Glu Asp Phe Asp Ile Leu Cys Thr His Pro Met Phe 180 185 190 Gly Pro Gln Ser Val Ser Ser Asn His Gly Trp Arg Gly Leu Arg Phe 195 200 205 Val Tyr Asp Lys Val Arg Ile Gly Glu Glu Arg Leu Arg Val Ser Arg 210 215 220 Cys Glu Ser Phe Leu Glu Ile Phe Val Arg Glu Gly Cys Glu Met Val 225 230 235 240 Glu Met Ser Val Thr Asp His Asp Lys Phe Ala Ala Glu Ser Gln Phe 245 250 255 Ile Thr His Thr Leu Gly Arg Leu Leu Gly Met Leu Lys Leu Ile Ser 260 265 270 Thr Pro Ile Asn Thr Lys Gly Tyr Glu Ala Leu Leu Asp Leu Ala Glu 275 280 285 Asn Ile Cys Gly Asp Ser Phe Asp Leu Tyr Tyr Gly Leu Phe Val Tyr 290 295 300 Asn Asn Asn Ser Leu Glu Val Leu Glu Arg Ile Asp Leu Ala Phe Glu 305 310 315 320 Ala Leu Arg Lys Glu Leu Phe Ser Arg Leu His Gly Val Val Arg Lys 325 330 335 Gln Ser Phe Glu Gly Glu Ala Lys Lys Val His Val Phe Pro Asn Cys 340 345 350 Gly Glu Asn Asp Ala Ser Leu Asp Met Met Arg Ser Glu Asp Val Val 355 360 365 Val Lys Tyr Glu Tyr Asn Ser Gln Val Ser Gly Ser Val Asn Asp Gly 370 375 380 Ser Arg Leu Lys Ile Gly Ile Val Gly Phe Gly Asn Phe Gly Gln Phe 385 390 395 400 Leu Gly Lys Thr Met Val Lys Gln Gly His Thr Val Leu Ala Tyr Ser 405 410 415 Arg Ser Asp Tyr Thr Asp Glu Ala Ala Lys Leu Gly Val Ser Tyr Phe 420 425 430 Ser Asp Leu Asp Asp Leu Phe Glu Glu His Pro Glu Val Ile Ile Leu 435 440 445 Cys Thr Ser Ile Leu Ser Thr Glu Lys Val Leu Glu Ser Leu Pro Phe 450 455 460 Gln Arg Leu Lys Arg Ser Thr Leu Phe Val Asp Val Leu Ser Val Lys 465 470 475 480 Glu Phe Pro Arg Asn Leu Phe Leu Gln Thr Leu Pro Gln Asp Phe Asp 485 490 495 Ile Leu Cys Thr His Pro Met Phe Gly Pro Glu Ser Gly Lys Asn Gly 500 505 510 Trp Asn Asn Leu Ala Phe Val Phe Asp Lys Val Arg Ile Gly Met Asp 515 520 525 Asp Arg Arg Lys Ser Arg Cys Asn Ser Phe Leu Asp Ile Phe Ala Arg 530 535 540 Glu Gly Cys Arg Met Val Glu Met Ser Cys Ala Glu His Asp Trp His 545 550 555 560 Ala Ala Gly Ser Gln Phe Ile Thr His Thr Val Gly Arg Leu Leu Glu 565 570 575 Lys Leu Ser Leu Glu Ser Thr Pro Ile Asp Thr Lys Gly Tyr Glu Thr 580 585 590 Leu Leu Lys Leu Val Glu Asn Thr Ala Gly Asp Ser Phe Asp Leu Tyr 595 600 605 Tyr Gly Leu Phe Leu Tyr Asn Pro Asn Ala Met Glu Gln Leu Glu Arg 610 615 620 Phe His Val Ala Phe Glu Ser Leu Lys Thr Gln Leu Phe Gly Arg Leu 625 630 635 640 His Ser Gln His Ser His Glu Leu Ala Lys Ser Ser Ser Pro Lys Thr 645 650 655 Thr Lys Leu Leu 660 4 933 DNA Arabidopsis thaliana CDS (1)..(933) 4 atg acc gac acc atc cct ctt ccc aac tcc aac tcc aac gcc acc cct 48 Met Thr Asp Thr Ile Pro Leu Pro Asn Ser Asn Ser Asn Ala Thr Pro 1 5 10 15 cct ctc cgt atc gcc atc atc gga ttc gga aac tac ggc caa ttc ctt 96 Pro Leu Arg Ile Ala Ile Ile Gly Phe Gly Asn Tyr Gly Gln Phe Leu 20 25 30 gcc gaa acc cta att tct caa ggc cac att ctc ttc gct cac tcc cga 144 Ala Glu Thr Leu Ile Ser Gln Gly His Ile Leu Phe Ala His Ser Arg 35 40 45 tcc gat cac tcc tcc gcc gct cgc cgt ctc ggt gtc tca tac ttc acc 192 Ser Asp His Ser Ser Ala Ala Arg Arg Leu Gly Val Ser Tyr Phe Thr 50 55 60 gat ctt cac gat ctc tgc gaa cgt cat cct gac gta gtc ctt ctc tgt 240 Asp Leu His Asp Leu Cys Glu Arg His Pro Asp Val Val Leu Leu Cys 65 70 75 80 act tca atc ctc tcc ata gag aat att ctc aaa acg ttg ccg ttt cag 288 Thr Ser Ile Leu Ser Ile Glu Asn Ile Leu Lys Thr Leu Pro Phe Gln 85 90 95 aga ctc cgt cgc aac act ctc ttc gtt gat gtt ctc tcc gtt aaa gag 336 Arg Leu Arg Arg Asn Thr Leu Phe Val Asp Val Leu Ser Val Lys Glu 100 105 110 ttt gct aaa act ctt ctc ctt caa tac tta cct gaa gat ttc gat att 384 Phe Ala Lys Thr Leu Leu Leu Gln Tyr Leu Pro Glu Asp Phe Asp Ile 115 120 125 ctt tgt aca cat cca atg ttt ggt cct cag agt gtg agt tca aat cat 432 Leu Cys Thr His Pro Met Phe Gly Pro Gln Ser Val Ser Ser Asn His 130 135 140 ggc tgg aga gga tta aga ttt gtg tat gat aaa gtt agg att ggg gaa 480 Gly Trp Arg Gly Leu Arg Phe Val Tyr Asp Lys Val Arg Ile Gly Glu 145 150 155 160 gag aga ttg aga gtc tca agg tgt gag agt ttt ctt gag att ttt gtt 528 Glu Arg Leu Arg Val Ser Arg Cys Glu Ser Phe Leu Glu Ile Phe Val 165 170 175 aga gaa gga tgt gag atg gtg gag atg agt gtt act gat cat gat aag 576 Arg Glu Gly Cys Glu Met Val Glu Met Ser Val Thr Asp His Asp Lys 180 185 190 ttt gct gct gaa tca cag ttt ata act cat act ctt ggt agg ctt ttg 624 Phe Ala Ala Glu Ser Gln Phe Ile Thr His Thr Leu Gly Arg Leu Leu 195 200 205 ggg atg ttg aag ttg ata tcg acg ccg att aat acg aaa ggg tac gag 672 Gly Met Leu Lys Leu Ile Ser Thr Pro Ile Asn Thr Lys Gly Tyr Glu 210 215 220 gcg ttg ctt gat tta gct gag aat att tgt ggg gat agt ttt gat ttg 720 Ala Leu Leu Asp Leu Ala Glu Asn Ile Cys Gly Asp Ser Phe Asp Leu 225 230 235 240 tat tat ggg ttg ttt gtg tat aat aac aac tct ttg gag gtg tta gag 768 Tyr Tyr Gly Leu Phe Val Tyr Asn Asn Asn Ser Leu Glu Val Leu Glu 245 250 255 agg att gat ttg gct ttc gag gct ttg cgt aag gag ctt ttt agt cgg 816 Arg Ile Asp Leu Ala Phe Glu Ala Leu Arg Lys Glu Leu Phe Ser Arg 260 265 270 ctt cac ggt gtt gtg agg aag cag tct ttt gaa ggt gaa gca aag aaa 864 Leu His Gly Val Val Arg Lys Gln Ser Phe Glu Gly Glu Ala Lys Lys 275 280 285 gtt cat gtt ttt cca aat tgt ggt gaa aat gat gct tct ttg gat atg 912 Val His Val Phe Pro Asn Cys Gly Glu Asn Asp Ala Ser Leu Asp Met 290 295 300 atg agg tat gta gtt agt tag 933 Met Arg Tyr Val Val Ser 305 310 5 310 PRT Arabidopsis thaliana 5 Met Thr Asp Thr Ile Pro Leu Pro Asn Ser Asn Ser Asn Ala Thr Pro 1 5 10 15 Pro Leu Arg Ile Ala Ile Ile Gly Phe Gly Asn Tyr Gly Gln Phe Leu 20 25 30 Ala Glu Thr Leu Ile Ser Gln Gly His Ile Leu Phe Ala His Ser Arg 35 40 45 Ser Asp His Ser Ser Ala Ala Arg Arg Leu Gly Val Ser Tyr Phe Thr 50 55 60 Asp Leu His Asp Leu Cys Glu Arg His Pro Asp Val Val Leu Leu Cys 65 70 75 80 Thr Ser Ile Leu Ser Ile Glu Asn Ile Leu Lys Thr Leu Pro Phe Gln 85 90 95 Arg Leu Arg Arg Asn Thr Leu Phe Val Asp Val Leu Ser Val Lys Glu 100 105 110 Phe Ala Lys Thr Leu Leu Leu Gln Tyr Leu Pro Glu Asp Phe Asp Ile 115 120 125 Leu Cys Thr His Pro Met Phe Gly Pro Gln Ser Val Ser Ser Asn His 130 135 140 Gly Trp Arg Gly Leu Arg Phe Val Tyr Asp Lys Val Arg Ile Gly Glu 145 150 155 160 Glu Arg Leu Arg Val Ser Arg Cys Glu Ser Phe Leu Glu Ile Phe Val 165 170 175 Arg Glu Gly Cys Glu Met Val Glu Met Ser Val Thr Asp His Asp Lys 180 185 190 Phe Ala Ala Glu Ser Gln Phe Ile Thr His Thr Leu Gly Arg Leu Leu 195 200 205 Gly Met Leu Lys Leu Ile Ser Thr Pro Ile Asn Thr Lys Gly Tyr Glu 210 215 220 Ala Leu Leu Asp Leu Ala Glu Asn Ile Cys Gly Asp Ser Phe Asp Leu 225 230 235 240 Tyr Tyr Gly Leu Phe Val Tyr Asn Asn Asn Ser Leu Glu Val Leu Glu 245 250 255 Arg Ile Asp Leu Ala Phe Glu Ala Leu Arg Lys Glu Leu Phe Ser Arg 260 265 270 Leu His Gly Val Val Arg Lys Gln Ser Phe Glu Gly Glu Ala Lys Lys 275 280 285 Val His Val Phe Pro Asn Cys Gly Glu Asn Asp Ala Ser Leu Asp Met 290 295 300 Met Arg Tyr Val Val Ser 305 310 6 909 DNA Arabidopsis thaliana CDS (1)..(909) 6 atg atg agg tca gaa gat gtt gtt gtg aag tat gaa tat aac tcc cag 48 Met Met Arg Ser Glu Asp Val Val Val Lys Tyr Glu Tyr Asn Ser Gln 1 5 10 15 gtg tct ggt agt gtt aat gac ggt tcg agg ctc aag att ggt atc gtc 96 Val Ser Gly Ser Val Asn Asp Gly Ser Arg Leu Lys Ile Gly Ile Val 20 25 30 ggg ttt gga aat ttt gga cag ttt cta ggt aaa acc atg gtc aag cag 144 Gly Phe Gly Asn Phe Gly Gln Phe Leu Gly Lys Thr Met Val Lys Gln 35 40 45 ggt cac act gtg tta gct tat tcc aga agt gac tac act gat gaa gca 192 Gly His Thr Val Leu Ala Tyr Ser Arg Ser Asp Tyr Thr Asp Glu Ala 50 55 60 gca aag ctc ggt gtt tcg tat ttt tca gat ctt gat gat cta ttt gaa 240 Ala Lys Leu Gly Val Ser Tyr Phe Ser Asp Leu Asp Asp Leu Phe Glu 65 70 75 80 gag cat cct gaa gtt att att ctc tgt acg tca atc ctt tcg act gaa 288 Glu His Pro Glu Val Ile Ile Leu Cys Thr Ser Ile Leu Ser Thr Glu 85 90 95 aaa gtt ctc gag tca cta ccg ttt cag aga ctg aag aga agc aca ctt 336 Lys Val Leu Glu Ser Leu Pro Phe Gln Arg Leu Lys Arg Ser Thr Leu 100 105 110 ttt gtg gat gta ctc tca gta aaa gag ttc ccg agg aat tta ttt ctt 384 Phe Val Asp Val Leu Ser Val Lys Glu Phe Pro Arg Asn Leu Phe Leu 115 120 125 caa act ctc cca caa gat ttt gat att ttg tgc acg cat cct atg ttt 432 Gln Thr Leu Pro Gln Asp Phe Asp Ile Leu Cys Thr His Pro Met Phe 130 135 140 ggg cca gag agt ggt aaa aat gga tgg aac aat ctt gcc ttt gtg ttt 480 Gly Pro Glu Ser Gly Lys Asn Gly Trp Asn Asn Leu Ala Phe Val Phe 145 150 155 160 gat aag gtt agg att gga atg gat gat aga aga aaa tcg agg tgt aac 528 Asp Lys Val Arg Ile Gly Met Asp Asp Arg Arg Lys Ser Arg Cys Asn 165 170 175 agt ttt ctt gat att ttt gcc cgt gaa gga tgt cgt atg gtg gag atg 576 Ser Phe Leu Asp Ile Phe Ala Arg Glu Gly Cys Arg Met Val Glu Met 180 185 190 tcg tgt gct gaa cat gat tgg cat gct gct gga tca cag ttt atc aca 624 Ser Cys Ala Glu His Asp Trp His Ala Ala Gly Ser Gln Phe Ile Thr 195 200 205 cac aca gtg gga agg ctt ctg gag aag ctg agc ttg gaa tct act cct 672 His Thr Val Gly Arg Leu Leu Glu Lys Leu Ser Leu Glu Ser Thr Pro 210 215 220 ata gat acc aaa ggt tat gag aca ttg cta aaa ctg gtg gag aat act 720 Ile Asp Thr Lys Gly Tyr Glu Thr Leu Leu Lys Leu Val Glu Asn Thr 225 230 235 240 gct ggt gac agc ttt gat ctg tac tat gga cta ttt tta tac aat cct 768 Ala Gly Asp Ser Phe Asp Leu Tyr Tyr Gly Leu Phe Leu Tyr Asn Pro 245 250 255 aat gca atg gaa cag ctt gag agg ttt cat gtg gct ttt gaa tca ttg 816 Asn Ala Met Glu Gln Leu Glu Arg Phe His Val Ala Phe Glu Ser Leu 260 265 270 aag aca cag ctc ttt gga cga cta cat tct caa cat tct cat gag cta 864 Lys Thr Gln Leu Phe Gly Arg Leu His Ser Gln His Ser His Glu Leu 275 280 285 gct aaa tca tct tcc cca aag aca act aag cta tta act agc taa 909 Ala Lys Ser Ser Ser Pro Lys Thr Thr Lys Leu Leu Thr Ser 290 295 300 7 302 PRT Arabidopsis thaliana 7 Met Met Arg Ser Glu Asp Val Val Val Lys Tyr Glu Tyr Asn Ser Gln 1 5 10 15 Val Ser Gly Ser Val Asn Asp Gly Ser Arg Leu Lys Ile Gly Ile Val 20 25 30 Gly Phe Gly Asn Phe Gly Gln Phe Leu Gly Lys Thr Met Val Lys Gln 35 40 45 Gly His Thr Val Leu Ala Tyr Ser Arg Ser Asp Tyr Thr Asp Glu Ala 50 55 60 Ala Lys Leu Gly Val Ser Tyr Phe Ser Asp Leu Asp Asp Leu Phe Glu 65 70 75 80 Glu His Pro Glu Val Ile Ile Leu Cys Thr Ser Ile Leu Ser Thr Glu 85 90 95 Lys Val Leu Glu Ser Leu Pro Phe Gln Arg Leu Lys Arg Ser Thr Leu 100 105 110 Phe Val Asp Val Leu Ser Val Lys Glu Phe Pro Arg Asn Leu Phe Leu 115 120 125 Gln Thr Leu Pro Gln Asp Phe Asp Ile Leu Cys Thr His Pro Met Phe 130 135 140 Gly Pro Glu Ser Gly Lys Asn Gly Trp Asn Asn Leu Ala Phe Val Phe 145 150 155 160 Asp Lys Val Arg Ile Gly Met Asp Asp Arg Arg Lys Ser Arg Cys Asn 165 170 175 Ser Phe Leu Asp Ile Phe Ala Arg Glu Gly Cys Arg Met Val Glu Met 180 185 190 Ser Cys Ala Glu His Asp Trp His Ala Ala Gly Ser Gln Phe Ile Thr 195 200 205 His Thr Val Gly Arg Leu Leu Glu Lys Leu Ser Leu Glu Ser Thr Pro 210 215 220 Ile Asp Thr Lys Gly Tyr Glu Thr Leu Leu Lys Leu Val Glu Asn Thr 225 230 235 240 Ala Gly Asp Ser Phe Asp Leu Tyr Tyr Gly Leu Phe Leu Tyr Asn Pro 245 250 255 Asn Ala Met Glu Gln Leu Glu Arg Phe His Val Ala Phe Glu Ser Leu 260 265 270 Lys Thr Gln Leu Phe Gly Arg Leu His Ser Gln His Ser His Glu Leu 275 280 285 Ala Lys Ser Ser Ser Pro Lys Thr Thr Lys Leu Leu Thr Ser 290 295 300 8 1077 DNA Arabidopsis thaliana CDS (1)..(1077) 8 atg cta ctc cat ttc tct ccg gcg aaa ccc ctc att tct cca ccc aat 48 Met Leu Leu His Phe Ser Pro Ala Lys Pro Leu Ile Ser Pro Pro Asn 1 5 10 15 ctc cgc cgc aat tca ccc aca ttc ctc att tcc ccg ccg cga tct ctt 96 Leu Arg Arg Asn Ser Pro Thr Phe Leu Ile Ser Pro Pro Arg Ser Leu 20 25 30 cga att cga gca atc gac gcc gcc caa atc ttc gat tac gaa acc caa 144 Arg Ile Arg Ala Ile Asp Ala Ala Gln Ile Phe Asp Tyr Glu Thr Gln 35 40 45 ctc aaa tcc gag tac cgc aaa tcc tct gct ctc aaa atc gcc gtc ttg 192 Leu Lys Ser Glu Tyr Arg Lys Ser Ser Ala Leu Lys Ile Ala Val Leu 50 55 60 ggt ttc ggc aat ttc ggc caa ttc ctc tcc aaa acc cta att cga cac 240 Gly Phe Gly Asn Phe Gly Gln Phe Leu Ser Lys Thr Leu Ile Arg His 65 70 75 80 ggc cac gat cta atc act cac tcc cgc tcc gat tac tcc gac gcc gca 288 Gly His Asp Leu Ile Thr His Ser Arg Ser Asp Tyr Ser Asp Ala Ala 85 90 95 aac tca atc gga gct cgt ttc ttc gat aac cct cac gat ctc tgt gaa 336 Asn Ser Ile Gly Ala Arg Phe Phe Asp Asn Pro His Asp Leu Cys Glu 100 105 110 caa cat ccc gac gtt gtc ctc ctc tgt acc tca atc ctc tcc aca gaa 384 Gln His Pro Asp Val Val Leu Leu Cys Thr Ser Ile Leu Ser Thr Glu 115 120 125 tca gtc ctc aga tca ttc cct ttc caa cgt ctc cgt cgt agc aca ctc 432 Ser Val Leu Arg Ser Phe Pro Phe Gln Arg Leu Arg Arg Ser Thr Leu 130 135 140 ttc gtc gat gtt ctc tcc gtt aag gaa ttc cca aaa gcc ctc ttc att 480 Phe Val Asp Val Leu Ser Val Lys Glu Phe Pro Lys Ala Leu Phe Ile 145 150 155 160 aaa tac ctt cct aag gag ttt gac att ctc tgt act cat cca atg ttt 528 Lys Tyr Leu Pro Lys Glu Phe Asp Ile Leu Cys Thr His Pro Met Phe 165 170 175 gga cct gag agt ggt aag cat tct tgg tct ggc ttg ccc ttt gtc tac 576 Gly Pro Glu Ser Gly Lys His Ser Trp Ser Gly Leu Pro Phe Val Tyr 180 185 190 gat aag gtg aga atc gga gac gca gct tca aga caa gag agg tgt gag 624 Asp Lys Val Arg Ile Gly Asp Ala Ala Ser Arg Gln Glu Arg Cys Glu 195 200 205 aag ttt cta aga att ttt gag aat gaa ggt tgc aag atg gtt gaa atg 672 Lys Phe Leu Arg Ile Phe Glu Asn Glu Gly Cys Lys Met Val Glu Met 210 215 220 agc tgt gag aag cat gat tat tac gca gct gga tcg caa ttc gtg acg 720 Ser Cys Glu Lys His Asp Tyr Tyr Ala Ala Gly Ser Gln Phe Val Thr 225 230 235 240 cat act atg gga agg gtt ttg gag aaa tat gga gtt gag tct tcg ccg 768 His Thr Met Gly Arg Val Leu Glu Lys Tyr Gly Val Glu Ser Ser Pro 245 250 255 att aac acc aaa ggt tat gag acg ttg ttg gat ttg gtg gag aac aca 816 Ile Asn Thr Lys Gly Tyr Glu Thr Leu Leu Asp Leu Val Glu Asn Thr 260 265 270 tcg agt gat agc ttt gag ctt ttc tac ggt ttg ttt atg tat aat ccg 864 Ser Ser Asp Ser Phe Glu Leu Phe Tyr Gly Leu Phe Met Tyr Asn Pro 275 280 285 aat gct ctt gaa cag ttg gag aga ttg gat atg gct ttt gag tct gtt 912 Asn Ala Leu Glu Gln Leu Glu Arg Leu Asp Met Ala Phe Glu Ser Val 290 295 300 aag aag gag ctg ttt ggg aga tta cat cag caa tac agg aag caa atg 960 Lys Lys Glu Leu Phe Gly Arg Leu His Gln Gln Tyr Arg Lys Gln Met 305 310 315 320 ttt ggt ggg gag gtt caa tcg ccc aag aaa act gag cag aaa ttg ctc 1008 Phe Gly Gly Glu Val Gln Ser Pro Lys Lys Thr Glu Gln Lys Leu Leu 325 330 335 aat gat ggt ggt gtt gtt cct atg aat gat ata tca tca tca tca tca 1056 Asn Asp Gly Gly Val Val Pro Met Asn Asp Ile Ser Ser Ser Ser Ser 340 345 350 tca tca tca tca tca tct taa 1077 Ser Ser Ser Ser Ser Ser 355 9 358 PRT Arabidopsis thaliana 9 Met Leu Leu His Phe Ser Pro Ala Lys Pro Leu Ile Ser Pro Pro Asn 1 5 10 15 Leu Arg Arg Asn Ser Pro Thr Phe Leu Ile Ser Pro Pro Arg Ser Leu 20 25 30 Arg Ile Arg Ala Ile Asp Ala Ala Gln Ile Phe Asp Tyr Glu Thr Gln 35 40 45 Leu Lys Ser Glu Tyr Arg Lys Ser Ser Ala Leu Lys Ile Ala Val Leu 50 55 60 Gly Phe Gly Asn Phe Gly Gln Phe Leu Ser Lys Thr Leu Ile Arg His 65 70 75 80 Gly His Asp Leu Ile Thr His Ser Arg Ser Asp Tyr Ser Asp Ala Ala 85 90 95 Asn Ser Ile Gly Ala Arg Phe Phe Asp Asn Pro His Asp Leu Cys Glu 100 105 110 Gln His Pro Asp Val Val Leu Leu Cys Thr Ser Ile Leu Ser Thr Glu 115 120 125 Ser Val Leu Arg Ser Phe Pro Phe Gln Arg Leu Arg Arg Ser Thr Leu 130 135 140 Phe Val Asp Val Leu Ser Val Lys Glu Phe Pro Lys Ala Leu Phe Ile 145 150 155 160 Lys Tyr Leu Pro Lys Glu Phe Asp Ile Leu Cys Thr His Pro Met Phe 165 170 175 Gly Pro Glu Ser Gly Lys His Ser Trp Ser Gly Leu Pro Phe Val Tyr 180 185 190 Asp Lys Val Arg Ile Gly Asp Ala Ala Ser Arg Gln Glu Arg Cys Glu 195 200 205 Lys Phe Leu Arg Ile Phe Glu Asn Glu Gly Cys Lys Met Val Glu Met 210 215 220 Ser Cys Glu Lys His Asp Tyr Tyr Ala Ala Gly Ser Gln Phe Val Thr 225 230 235 240 His Thr Met Gly Arg Val Leu Glu Lys Tyr Gly Val Glu Ser Ser Pro 245 250 255 Ile Asn Thr Lys Gly Tyr Glu Thr Leu Leu Asp Leu Val Glu Asn Thr 260 265 270 Ser Ser Asp Ser Phe Glu Leu Phe Tyr Gly Leu Phe Met Tyr Asn Pro 275 280 285 Asn Ala Leu Glu Gln Leu Glu Arg Leu Asp Met Ala Phe Glu Ser Val 290 295 300 Lys Lys Glu Leu Phe Gly Arg Leu His Gln Gln Tyr Arg Lys Gln Met 305 310 315 320 Phe Gly Gly Glu Val Gln Ser Pro Lys Lys Thr Glu Gln Lys Leu Leu 325 330 335 Asn Asp Gly Gly Val Val Pro Met Asn Asp Ile Ser Ser Ser Ser Ser 340 345 350 Ser Ser Ser Ser Ser Ser 355 10 1476 DNA Picea glauca CDS (96)..(980) 10 accagtttta gatattcatc aaggtcttgc ctgctttgtt ttaggcaatt ccctccagta 60 ccaagccctc ttctcagaaa actccctccg cggca atg cct ctt cat ttc tca 113 Met Pro Leu His Phe Ser 1 5 tgg aat cca aca gaa gac cct cac aca gta cgc cct act gag gct ctc 161 Trp Asn Pro Thr Glu Asp Pro His Thr Val Arg Pro Thr Glu Ala Leu 10 15 20 agg aat cag agc aat gga cgt cgc ggg gcc cct cga tta aga aga ata 209 Arg Asn Gln Ser Asn Gly Arg Arg Gly Ala Pro Arg Leu Arg Arg Ile 25 30 35 aaa tcc att aaa tat tgg cat cgt agg gtt tgg aaa cta cca cca att 257 Lys Ser Ile Lys Tyr Trp His Arg Arg Val Trp Lys Leu Pro Pro Ile 40 45 50 tct ggt gaa aac cat ggt gaa gcc ggg cca ccc ggt gct cgc cca ttc 305 Ser Gly Glu Asn His Gly Glu Ala Gly Pro Pro Gly Ala Arg Pro Phe 55 60 65 70 cag gac gga cta tac gga ggc cac tgc gag atc ggg gtt caa ttc ttc 353 Gln Asp Gly Leu Tyr Gly Gly His Cys Glu Ile Gly Val Gln Phe Phe 75 80 85 aga gac gcg gac gat ttc tgc gaa gag cat cca gag atc ata ctg atg 401 Arg Asp Ala Asp Asp Phe Cys Glu Glu His Pro Glu Ile Ile Leu Met 90 95 100 tgc gca tcc atc act ttg gtg gga gga cgt gct gaa gtc tct gcc aac 449 Cys Ala Ser Ile Thr Leu Val Gly Gly Arg Ala Glu Val Ser Ala Asn 105 110 115 aca gcg cct gaa gag gag tac gct ttt cgc aga cgt cct gtc tgt gaa 497 Thr Ala Pro Glu Glu Glu Tyr Ala Phe Arg Arg Arg Pro Val Cys Glu 120 125 130 aga gtt tcc gca ccg gtt gtt cct gca ggt ttt gtc gcc cga gtc gat 545 Arg Val Ser Ala Pro Val Val Pro Ala Gly Phe Val Ala Arg Val Asp 135 140 145 150 gtg ctg tgc act cat ccc atg ttt ggt cca gag agc agc aag gac gat 593 Val Leu Cys Thr His Pro Met Phe Gly Pro Glu Ser Ser Lys Asp Asp 155 160 165 ttg ggc gac ctc cct ttc gtt tac gat aag gtt agg gtt tct aac gaa 641 Leu Gly Asp Leu Pro Phe Val Tyr Asp Lys Val Arg Val Ser Asn Glu 170 175 180 ggt ttg aga gcc aag cac tgc gag cgt ttt ctc aac ata ttt tcg tgc 689 Gly Leu Arg Ala Lys His Cys Glu Arg Phe Leu Asn Ile Phe Ser Cys 185 190 195 gag ggc tgc cgg atg gtc gag atg tcg tgt gca gaa cat gat cgc tat 737 Glu Gly Cys Arg Met Val Glu Met Ser Cys Ala Glu His Asp Arg Tyr 200 205 210 gtc gcg gag agc caa ttc att acc cac acc gtt ggg agg atg ttg ggg 785 Val Ala Glu Ser Gln Phe Ile Thr His Thr Val Gly Arg Met Leu Gly 215 220 225 230 agg ctg ggc ttg gag tcc act ccg att gct acc aag ggt tat gag aaa 833 Arg Leu Gly Leu Glu Ser Thr Pro Ile Ala Thr Lys Gly Tyr Glu Lys 235 240 245 tta ctg gaa gtg gcc tgg aat att gcc ggg gat agt ttt gat att tat 881 Leu Leu Glu Val Ala Trp Asn Ile Ala Gly Asp Ser Phe Asp Ile Tyr 250 255 260 tat gga ctc ttc atg tat aat gtc aat tcg att gaa caa atc gag agg 929 Tyr Gly Leu Phe Met Tyr Asn Val Asn Ser Ile Glu Gln Ile Glu Arg 265 270 275 tta gat atg gcg ttc aat tca ctc aag aac gag gtt tcg ggt tca aat 977 Leu Asp Met Ala Phe Asn Ser Leu Lys Asn Glu Val Ser Gly Ser Asn 280 285 290 taa gaattttaaa ggtttcgatt tgcttgaagc ggcttgtgta tgaagtacca 1030 tttgtagaca ataatgaatt cgagaatgtt gttcaagatg aaatggttaa gaaggatggg 1090 tctcgtgtga gaagaaaacc aagataaatg gttgcgtagt ggtccagaaa tctgcattca 1150 ttactgaatg attctacatg gagtgagtaa gcattgattg aattccaaga cgagtgaaag 1210 agtttgatga atggaatatg tctgtattcc aaatttaata aatgaaaaat attgcaggtt 1270 gctatatgca atggttcttc tatatccccg aaggacaaat gacagatata agttctctgg 1330 cacttgtcag aaaacttcta tgtttgtagc cataaaacat tttccgaaag tggaactttt 1390 ctagaactta taggggaaat aatccctatg caaacactgt atgagtccca ttgacctttc 1450 tttctcattt catttcattt ttgtct 1476 11 294 PRT Picea glauca 11 Met Pro Leu His Phe Ser Trp Asn Pro Thr Glu Asp Pro His Thr Val 1 5 10 15 Arg Pro Thr Glu Ala Leu Arg Asn Gln Ser Asn Gly Arg Arg Gly Ala 20 25 30 Pro Arg Leu Arg Arg Ile Lys Ser Ile Lys Tyr Trp His Arg Arg Val 35 40 45 Trp Lys Leu Pro Pro Ile Ser Gly Glu Asn His Gly Glu Ala Gly Pro 50 55 60 Pro Gly Ala Arg Pro Phe Gln Asp Gly Leu Tyr Gly Gly His Cys Glu 65 70 75 80 Ile Gly Val Gln Phe Phe Arg Asp Ala Asp Asp Phe Cys Glu Glu His 85 90 95 Pro Glu Ile Ile Leu Met Cys Ala Ser Ile Thr Leu Val Gly Gly Arg 100 105 110 Ala Glu Val Ser Ala Asn Thr Ala Pro Glu Glu Glu Tyr Ala Phe Arg 115 120 125 Arg Arg Pro Val Cys Glu Arg Val Ser Ala Pro Val Val Pro Ala Gly 130 135 140 Phe Val Ala Arg Val Asp Val Leu Cys Thr His Pro Met Phe Gly Pro 145 150 155 160 Glu Ser Ser Lys Asp Asp Leu Gly Asp Leu Pro Phe Val Tyr Asp Lys 165 170 175 Val Arg Val Ser Asn Glu Gly Leu Arg Ala Lys His Cys Glu Arg Phe 180 185 190 Leu Asn Ile Phe Ser Cys Glu Gly Cys Arg Met Val Glu Met Ser Cys 195 200 205 Ala Glu His Asp Arg Tyr Val Ala Glu Ser Gln Phe Ile Thr His Thr 210 215 220 Val Gly Arg Met Leu Gly Arg Leu Gly Leu Glu Ser Thr Pro Ile Ala 225 230 235 240 Thr Lys Gly Tyr Glu Lys Leu Leu Glu Val Ala Trp Asn Ile Ala Gly 245 250 255 Asp Ser Phe Asp Ile Tyr Tyr Gly Leu Phe Met Tyr Asn Val Asn Ser 260 265 270 Ile Glu Gln Ile Glu Arg Leu Asp Met Ala Phe Asn Ser Leu Lys Asn 275 280 285 Glu Val Ser Gly Ser Asn 290 12 840 DNA Synechocystis sp. CDS (1)..(840) 12 atg aaa att ggt gtt gtt ggt ttg ggt tta att ggg gct tcc ttg gcg 48 Met Lys Ile Gly Val Val Gly Leu Gly Leu Ile Gly Ala Ser Leu Ala 1 5 10 15 gga gac ttg cgt cgt cgg ggc cat tat ttg att ggg gtt tct cgg caa 96 Gly Asp Leu Arg Arg Arg Gly His Tyr Leu Ile Gly Val Ser Arg Gln 20 25 30 caa agc acc tgt gaa aaa gca gtg gaa aga caa ttg gtg gat gaa gcg 144 Gln Ser Thr Cys Glu Lys Ala Val Glu Arg Gln Leu Val Asp Glu Ala 35 40 45 ggt caa gat tta tct ctt ctc caa aca gca aaa ata att ttt ctt tgt 192 Gly Gln Asp Leu Ser Leu Leu Gln Thr Ala Lys Ile Ile Phe Leu Cys 50 55 60 act cct ata caa tta att ttg cct acc cta gag aag ctt att ccc cat 240 Thr Pro Ile Gln Leu Ile Leu Pro Thr Leu Glu Lys Leu Ile Pro His 65 70 75 80 cta tcg ccc aca gcc att gtc act gat gtg gcc tct gta aaa acg gcg 288 Leu Ser Pro Thr Ala Ile Val Thr Asp Val Ala Ser Val Lys Thr Ala 85 90 95 atc gcc gag ccg gcc agt caa ctt tgg tct ggg ttc att ggt ggt cac 336 Ile Ala Glu Pro Ala Ser Gln Leu Trp Ser Gly Phe Ile Gly Gly His 100 105 110 ccc atg gcc ggc aca gcg gcc cag ggc atc gac ggg gcg gaa gaa aat 384 Pro Met Ala Gly Thr Ala Ala Gln Gly Ile Asp Gly Ala Glu Glu Asn 115 120 125 tta ttt gtc aac gct ccc tat gtg ctc act ccc acc gaa tat act gac 432 Leu Phe Val Asn Ala Pro Tyr Val Leu Thr Pro Thr Glu Tyr Thr Asp 130 135 140 cca gag caa ttg gct tgt tta cgt tca gtg ttg gaa ccc ctg ggg gta 480 Pro Glu Gln Leu Ala Cys Leu Arg Ser Val Leu Glu Pro Leu Gly Val 145 150 155 160 aaa att tac ctc tgc act ccc gca gac cat gac caa gca gta gcc tgg 528 Lys Ile Tyr Leu Cys Thr Pro Ala Asp His Asp Gln Ala Val Ala Trp 165 170 175 att tcc cat tta cct gta atg gtg agt gct gct tta atc caa gcc tgt 576 Ile Ser His Leu Pro Val Met Val Ser Ala Ala Leu Ile Gln Ala Cys 180 185 190 gcc ggt gaa aaa gat ggg gat att ctc aaa cta gcc caa aat ttg gcc 624 Ala Gly Glu Lys Asp Gly Asp Ile Leu Lys Leu Ala Gln Asn Leu Ala 195 200 205 agt tcg ggt ttt cgg gat acc agt cgg gtg gga ggc ggc aac ccg gag 672 Ser Ser Gly Phe Arg Asp Thr Ser Arg Val Gly Gly Gly Asn Pro Glu 210 215 220 ttg ggc acc atg atg gcc acc tat aac caa cgg gct ttg cta aaa agt 720 Leu Gly Thr Met Met Ala Thr Tyr Asn Gln Arg Ala Leu Leu Lys Ser 225 230 235 240 ttg caa gac tat cgt cag cac ctg gat cag cta att acc cta att agt 768 Leu Gln Asp Tyr Arg Gln His Leu Asp Gln Leu Ile Thr Leu Ile Ser 245 250 255 aac caa caa tgg cct gaa ctc cat cgt ctt tta caa caa acc aac ggc 816 Asn Gln Gln Trp Pro Glu Leu His Arg Leu Leu Gln Gln Thr Asn Gly 260 265 270 gat cgg gac aag tat gtt gaa taa 840 Asp Arg Asp Lys Tyr Val Glu 275 13 279 PRT Synechocystis sp. 13 Met Lys Ile Gly Val Val Gly Leu Gly Leu Ile Gly Ala Ser Leu Ala 1 5 10 15 Gly Asp Leu Arg Arg Arg Gly His Tyr Leu Ile Gly Val Ser Arg Gln 20 25 30 Gln Ser Thr Cys Glu Lys Ala Val Glu Arg Gln Leu Val Asp Glu Ala 35 40 45 Gly Gln Asp Leu Ser Leu Leu Gln Thr Ala Lys Ile Ile Phe Leu Cys 50 55 60 Thr Pro Ile Gln Leu Ile Leu Pro Thr Leu Glu Lys Leu Ile Pro His 65 70 75 80 Leu Ser Pro Thr Ala Ile Val Thr Asp Val Ala Ser Val Lys Thr Ala 85 90 95 Ile Ala Glu Pro Ala Ser Gln Leu Trp Ser Gly Phe Ile Gly Gly His 100 105 110 Pro Met Ala Gly Thr Ala Ala Gln Gly Ile Asp Gly Ala Glu Glu Asn 115 120 125 Leu Phe Val Asn Ala Pro Tyr Val Leu Thr Pro Thr Glu Tyr Thr Asp 130 135 140 Pro Glu Gln Leu Ala Cys Leu Arg Ser Val Leu Glu Pro Leu Gly Val 145 150 155 160 Lys Ile Tyr Leu Cys Thr Pro Ala Asp His Asp Gln Ala Val Ala Trp 165 170 175 Ile Ser His Leu Pro Val Met Val Ser Ala Ala Leu Ile Gln Ala Cys 180 185 190 Ala Gly Glu Lys Asp Gly Asp Ile Leu Lys Leu Ala Gln Asn Leu Ala 195 200 205 Ser Ser Gly Phe Arg Asp Thr Ser Arg Val Gly Gly Gly Asn Pro Glu 210 215 220 Leu Gly Thr Met Met Ala Thr Tyr Asn Gln Arg Ala Leu Leu Lys Ser 225 230 235 240 Leu Gln Asp Tyr Arg Gln His Leu Asp Gln Leu Ile Thr Leu Ile Ser 245 250 255 Asn Gln Gln Trp Pro Glu Leu His Arg Leu Leu Gln Gln Thr Asn Gly 260 265 270 Asp Arg Asp Lys Tyr Val Glu 275 14 1359 DNA Saccharomyces cerevisiae CDS (1)..(1359) 14 atg gta tca gag gat aag att gag caa tgg aaa gcc aca aaa gtc att 48 Met Val Ser Glu Asp Lys Ile Glu Gln Trp Lys Ala Thr Lys Val Ile 1 5 10 15 ggt ata att ggt ctg ggt gat atg ggc cta tta tac gct aat aaa ttt 96 Gly Ile Ile Gly Leu Gly Asp Met Gly Leu Leu Tyr Ala Asn Lys Phe 20 25 30 aca gat gct gga tgg ggt gtt ata tgt tgt gat agg gaa gaa tat tat 144 Thr Asp Ala Gly Trp Gly Val Ile Cys Cys Asp Arg Glu Glu Tyr Tyr 35 40 45 gat gaa ctg aaa gaa aaa tat gcc tca gct aaa ttc gaa ctg gtg aaa 192 Asp Glu Leu Lys Glu Lys Tyr Ala Ser Ala Lys Phe Glu Leu Val Lys 50 55 60 aat ggt cat ttg gta tcc agg caa agc gac tat att atc tat agt gtt 240 Asn Gly His Leu Val Ser Arg Gln Ser Asp Tyr Ile Ile Tyr Ser Val 65 70 75 80 gaa gca tcc aat att agt aag atc gtc gca acg tat gga cca tct tct 288 Glu Ala Ser Asn Ile Ser Lys Ile Val Ala Thr Tyr Gly Pro Ser Ser 85 90 95 aag gtt gga aca att gtt ggg ggt caa acg agt tgt aag ctg ccg gaa 336 Lys Val Gly Thr Ile Val Gly Gly Gln Thr Ser Cys Lys Leu Pro Glu 100 105 110 atc gag gct ttc gaa aag tat tta ccc aag gac tgc gac atc att acc 384 Ile Glu Ala Phe Glu Lys Tyr Leu Pro Lys Asp Cys Asp Ile Ile Thr 115 120 125 gtg cat tcc ctt cat ggg cct aaa gtt aat act gaa ggc caa cca cta 432 Val His Ser Leu His Gly Pro Lys Val Asn Thr Glu Gly Gln Pro Leu 130 135 140 gtt att atc aat cac aga tca cag tac cca gaa tct ttt gag ttc gtt 480 Val Ile Ile Asn His Arg Ser Gln Tyr Pro Glu Ser Phe Glu Phe Val 145 150 155 160 aat tct gtt atg gca tgt ttg aaa agt aag caa gtt tat ttg aca tat 528 Asn Ser Val Met Ala Cys Leu Lys Ser Lys Gln Val Tyr Leu Thr Tyr 165 170 175 gaa gag cat gac aag att acc gct gat aca caa gct gtg aca cat gct 576 Glu Glu His Asp Lys Ile Thr Ala Asp Thr Gln Ala Val Thr His Ala 180 185 190 gct ttc tta agt atg gga tct gcg tgg gca aag ata aag att tat cct 624 Ala Phe Leu Ser Met Gly Ser Ala Trp Ala Lys Ile Lys Ile Tyr Pro 195 200 205 tgg act ctg ggt gta aac aaa tgg tac ggt ggc cta gaa aat gtg aaa 672 Trp Thr Leu Gly Val Asn Lys Trp Tyr Gly Gly Leu Glu Asn Val Lys 210 215 220 gtt aat ata tca cta aga atc tat tcg aac aag tgg cat gtt tac gca 720 Val Asn Ile Ser Leu Arg Ile Tyr Ser Asn Lys Trp His Val Tyr Ala 225 230 235 240 gga tta gcc ata aca aac cca agt gca cat cag caa att ctt caa tat 768 Gly Leu Ala Ile Thr Asn Pro Ser Ala His Gln Gln Ile Leu Gln Tyr 245 250 255 gca acc agt gca aca gaa cta ttt agt tta atg ata gat aac aaa gaa 816 Ala Thr Ser Ala Thr Glu Leu Phe Ser Leu Met Ile Asp Asn Lys Glu 260 265 270 caa gaa ctt act gat aga cta tta aaa gct aag caa ttt gta ttt gga 864 Gln Glu Leu Thr Asp Arg Leu Leu Lys Ala Lys Gln Phe Val Phe Gly 275 280 285 aag cat act ggt ctc tta cta ttg gat gac acg att tta gag aaa tat 912 Lys His Thr Gly Leu Leu Leu Leu Asp Asp Thr Ile Leu Glu Lys Tyr 290 295 300 tcg cta tca aaa agc agc att ggt aac agc aac aat tgc aag cca gtg 960 Ser Leu Ser Lys Ser Ser Ile Gly Asn Ser Asn Asn Cys Lys Pro Val 305 310 315 320 ccg aat tca cat tta tca ttg ttg gcg att gtt gat tcg tgg ttt caa 1008 Pro Asn Ser His Leu Ser Leu Leu Ala Ile Val Asp Ser Trp Phe Gln 325 330 335 ctt ggt att gat cca tat gat cat atg att tgt tcg acg cca tta ttc 1056 Leu Gly Ile Asp Pro Tyr Asp His Met Ile Cys Ser Thr Pro Leu Phe 340 345 350 aga ata ttc ctg ggt gtg tcc gaa tat ctt ttt tta aaa cct ggc tta 1104 Arg Ile Phe Leu Gly Val Ser Glu Tyr Leu Phe Leu Lys Pro Gly Leu 355 360 365 tta gaa cag aca att gat gca gct atc cat gat aaa tca ttc ata aaa 1152 Leu Glu Gln Thr Ile Asp Ala Ala Ile His Asp Lys Ser Phe Ile Lys 370 375 380 gat gat tta gaa ttt gtt att tcg gct aga gaa tgg agc tcg gtt gtt 1200 Asp Asp Leu Glu Phe Val Ile Ser Ala Arg Glu Trp Ser Ser Val Val 385 390 395 400 tct ttt gcc aat ttt gat ata tac aaa aag caa ttt cag agt gtt caa 1248 Ser Phe Ala Asn Phe Asp Ile Tyr Lys Lys Gln Phe Gln Ser Val Gln 405 410 415 aag ttc ttt gag cca atg ctt cca gag gct aat ctc att ggc aac gag 1296 Lys Phe Phe Glu Pro Met Leu Pro Glu Ala Asn Leu Ile Gly Asn Glu 420 425 430 atg ata aaa acc att ctg agt cat tct agt gac cgt tcg gcc gct gaa 1344 Met Ile Lys Thr Ile Leu Ser His Ser Ser Asp Arg Ser Ala Ala Glu 435 440 445 aaa aga aat aca taa 1359 Lys Arg Asn Thr 450 15 452 PRT Saccharomyces cerevisiae 15 Met Val Ser Glu Asp Lys Ile Glu Gln Trp Lys Ala Thr Lys Val Ile 1 5 10 15 Gly Ile Ile Gly Leu Gly Asp Met Gly Leu Leu Tyr Ala Asn Lys Phe 20 25 30 Thr Asp Ala Gly Trp Gly Val Ile Cys Cys Asp Arg Glu Glu Tyr Tyr 35 40 45 Asp Glu Leu Lys Glu Lys Tyr Ala Ser Ala Lys Phe Glu Leu Val Lys 50 55 60 Asn Gly His Leu Val Ser Arg Gln Ser Asp Tyr Ile Ile Tyr Ser Val 65 70 75 80 Glu Ala Ser Asn Ile Ser Lys Ile Val Ala Thr Tyr Gly Pro Ser Ser 85 90 95 Lys Val Gly Thr Ile Val Gly Gly Gln Thr Ser Cys Lys Leu Pro Glu 100 105 110 Ile Glu Ala Phe Glu Lys Tyr Leu Pro Lys Asp Cys Asp Ile Ile Thr 115 120 125 Val His Ser Leu His Gly Pro Lys Val Asn Thr Glu Gly Gln Pro Leu 130 135 140 Val Ile Ile Asn His Arg Ser Gln Tyr Pro Glu Ser Phe Glu Phe Val 145 150 155 160 Asn Ser Val Met Ala Cys Leu Lys Ser Lys Gln Val Tyr Leu Thr Tyr 165 170 175 Glu Glu His Asp Lys Ile Thr Ala Asp Thr Gln Ala Val Thr His Ala 180 185 190 Ala Phe Leu Ser Met Gly Ser Ala Trp Ala Lys Ile Lys Ile Tyr Pro 195 200 205 Trp Thr Leu Gly Val Asn Lys Trp Tyr Gly Gly Leu Glu Asn Val Lys 210 215 220 Val Asn Ile Ser Leu Arg Ile Tyr Ser Asn Lys Trp His Val Tyr Ala 225 230 235 240 Gly Leu Ala Ile Thr Asn Pro Ser Ala His Gln Gln Ile Leu Gln Tyr 245 250 255 Ala Thr Ser Ala Thr Glu Leu Phe Ser Leu Met Ile Asp Asn Lys Glu 260 265 270 Gln Glu Leu Thr Asp Arg Leu Leu Lys Ala Lys Gln Phe Val Phe Gly 275 280 285 Lys His Thr Gly Leu Leu Leu Leu Asp Asp Thr Ile Leu Glu Lys Tyr 290 295 300 Ser Leu Ser Lys Ser Ser Ile Gly Asn Ser Asn Asn Cys Lys Pro Val 305 310 315 320 Pro Asn Ser His Leu Ser Leu Leu Ala Ile Val Asp Ser Trp Phe Gln 325 330 335 Leu Gly Ile Asp Pro Tyr Asp His Met Ile Cys Ser Thr Pro Leu Phe 340 345 350 Arg Ile Phe Leu Gly Val Ser Glu Tyr Leu Phe Leu Lys Pro Gly Leu 355 360 365 Leu Glu Gln Thr Ile Asp Ala Ala Ile His Asp Lys Ser Phe Ile Lys 370 375 380 Asp Asp Leu Glu Phe Val Ile Ser Ala Arg Glu Trp Ser Ser Val Val 385 390 395 400 Ser Phe Ala Asn Phe Asp Ile Tyr Lys Lys Gln Phe Gln Ser Val Gln 405 410 415 Lys Phe Phe Glu Pro Met Leu Pro Glu Ala Asn Leu Ile Gly Asn Glu 420 425 430 Met Ile Lys Thr Ile Leu Ser His Ser Ser Asp Arg Ser Ala Ala Glu 435 440 445 Lys Arg Asn Thr 450 16 1116 DNA Bacillus subtilis CDS (1)..(1116) 16 atg aat caa atg aaa gat aca ata ttg ctc gcc ggt ctc gga ttg ata 48 Met Asn Gln Met Lys Asp Thr Ile Leu Leu Ala Gly Leu Gly Leu Ile 1 5 10 15 ggc ggt tcg att gcc cta gcc atc aaa aaa aat cat ccc ggc aaa cgg 96 Gly Gly Ser Ile Ala Leu Ala Ile Lys Lys Asn His Pro Gly Lys Arg 20 25 30 att atc gga atc gac atc tct gat gaa cag gcg gta gcg gca tta aaa 144 Ile Ile Gly Ile Asp Ile Ser Asp Glu Gln Ala Val Ala Ala Leu Lys 35 40 45 tta ggc gtg ata gac gat cgt gct gat tcg ttt att agc ggt gtg aaa 192 Leu Gly Val Ile Asp Asp Arg Ala Asp Ser Phe Ile Ser Gly Val Lys 50 55 60 gag gca gct aca gta atc att gcg aca cct gtt gaa caa aca ctg gtt 240 Glu Ala Ala Thr Val Ile Ile Ala Thr Pro Val Glu Gln Thr Leu Val 65 70 75 80 atg ctt gaa gag ctg gct cat tca gga att gaa cat gag ctt ttg att 288 Met Leu Glu Glu Leu Ala His Ser Gly Ile Glu His Glu Leu Leu Ile 85 90 95 acg gat gta gga agc aca aag caa aaa gtg gtt gat tac gct gat caa 336 Thr Asp Val Gly Ser Thr Lys Gln Lys Val Val Asp Tyr Ala Asp Gln 100 105 110 gtg ctg cct agc cgc tat caa ttt gtc gga ggg cat ccg atg gcg ggt 384 Val Leu Pro Ser Arg Tyr Gln Phe Val Gly Gly His Pro Met Ala Gly 115 120 125 tca cat aaa tca gga gtg gcc gct gcg aag gag ttc ctg ttt gaa aat 432 Ser His Lys Ser Gly Val Ala Ala Ala Lys Glu Phe Leu Phe Glu Asn 130 135 140 gca ttt tat att tta acg cca ggc cag aaa acg gac aaa caa gct gtg 480 Ala Phe Tyr Ile Leu Thr Pro Gly Gln Lys Thr Asp Lys Gln Ala Val 145 150 155 160 gaa cag tta aaa aac ctg ctg aag ggg acg aat gcc cat ttt gtg gaa 528 Glu Gln Leu Lys Asn Leu Leu Lys Gly Thr Asn Ala His Phe Val Glu 165 170 175 atg tcg cca gag gag cat gat ggc gtt aca agc gta atc agt cat ttt 576 Met Ser Pro Glu Glu His Asp Gly Val Thr Ser Val Ile Ser His Phe 180 185 190 ccg cat att gta gca gct agc ctt gtt cac caa acc cat cat tcg gaa 624 Pro His Ile Val Ala Ala Ser Leu Val His Gln Thr His His Ser Glu 195 200 205 aac ctg tat ccg ctt gtt aag cgt ttt gct gcc ggc ggg ttc aga gat 672 Asn Leu Tyr Pro Leu Val Lys Arg Phe Ala Ala Gly Gly Phe Arg Asp 210 215 220 att aca agg att gca tca agc agc ccg gca atg tgg cgg gat att tta 720 Ile Thr Arg Ile Ala Ser Ser Ser Pro Ala Met Trp Arg Asp Ile Leu 225 230 235 240 tta cat aat aaa gat aaa atc tta gac cgt ttt gat gag tgg att cgt 768 Leu His Asn Lys Asp Lys Ile Leu Asp Arg Phe Asp Glu Trp Ile Arg 245 250 255 gaa att gac aag atc cgt aca tat gta gaa caa gaa gat gcg gaa aat 816 Glu Ile Asp Lys Ile Arg Thr Tyr Val Glu Gln Glu Asp Ala Glu Asn 260 265 270 cta ttt cgt tat ttt aaa aca gcc aag gat tat cgc gac ggg ctg ccg 864 Leu Phe Arg Tyr Phe Lys Thr Ala Lys Asp Tyr Arg Asp Gly Leu Pro 275 280 285 ctt cgg cag aag gga gcg ata cct gca ttt tat gat tta tat gtg gat 912 Leu Arg Gln Lys Gly Ala Ile Pro Ala Phe Tyr Asp Leu Tyr Val Asp 290 295 300 gta ccc gat cat ccg ggt gta ata tcc gag ata aca gcg atc tta gct 960 Val Pro Asp His Pro Gly Val Ile Ser Glu Ile Thr Ala Ile Leu Ala 305 310 315 320 gcg gag cgc atc agt atc acg aat atc cgc att atc gaa aca cga gag 1008 Ala Glu Arg Ile Ser Ile Thr Asn Ile Arg Ile Ile Glu Thr Arg Glu 325 330 335 gat att aac ggg att tta agg atc agt ttt cag tct gat gac gac cgc 1056 Asp Ile Asn Gly Ile Leu Arg Ile Ser Phe Gln Ser Asp Asp Asp Arg 340 345 350 aaa agg gca gaa caa tgc att gaa gcc cgg gcg gaa tat gaa act ttt 1104 Lys Arg Ala Glu Gln Cys Ile Glu Ala Arg Ala Glu Tyr Glu Thr Phe 355 360 365 tat gct gat tga 1116 Tyr Ala Asp 370 17 371 PRT Bacillus subtilis 17 Met Asn Gln Met Lys Asp Thr Ile Leu Leu Ala Gly Leu Gly Leu Ile 1 5 10 15 Gly Gly Ser Ile Ala Leu Ala Ile Lys Lys Asn His Pro Gly Lys Arg 20 25 30 Ile Ile Gly Ile Asp Ile Ser Asp Glu Gln Ala Val Ala Ala Leu Lys 35 40 45 Leu Gly Val Ile Asp Asp Arg Ala Asp Ser Phe Ile Ser Gly Val Lys 50 55 60 Glu Ala Ala Thr Val Ile Ile Ala Thr Pro Val Glu Gln Thr Leu Val 65 70 75 80 Met Leu Glu Glu Leu Ala His Ser Gly Ile Glu His Glu Leu Leu Ile 85 90 95 Thr Asp Val Gly Ser Thr Lys Gln Lys Val Val Asp Tyr Ala Asp Gln 100 105 110 Val Leu Pro Ser Arg Tyr Gln Phe Val Gly Gly His Pro Met Ala Gly 115 120 125 Ser His Lys Ser Gly Val Ala Ala Ala Lys Glu Phe Leu Phe Glu Asn 130 135 140 Ala Phe Tyr Ile Leu Thr Pro Gly Gln Lys Thr Asp Lys Gln Ala Val 145 150 155 160 Glu Gln Leu Lys Asn Leu Leu Lys Gly Thr Asn Ala His Phe Val Glu 165 170 175 Met Ser Pro Glu Glu His Asp Gly Val Thr Ser Val Ile Ser His Phe 180 185 190 Pro His Ile Val Ala Ala Ser Leu Val His Gln Thr His His Ser Glu 195 200 205 Asn Leu Tyr Pro Leu Val Lys Arg Phe Ala Ala Gly Gly Phe Arg Asp 210 215 220 Ile Thr Arg Ile Ala Ser Ser Ser Pro Ala Met Trp Arg Asp Ile Leu 225 230 235 240 Leu His Asn Lys Asp Lys Ile Leu Asp Arg Phe Asp Glu Trp Ile Arg 245 250 255 Glu Ile Asp Lys Ile Arg Thr Tyr Val Glu Gln Glu Asp Ala Glu Asn 260 265 270 Leu Phe Arg Tyr Phe Lys Thr Ala Lys Asp Tyr Arg Asp Gly Leu Pro 275 280 285 Leu Arg Gln Lys Gly Ala Ile Pro Ala Phe Tyr Asp Leu Tyr Val Asp 290 295 300 Val Pro Asp His Pro Gly Val Ile Ser Glu Ile Thr Ala Ile Leu Ala 305 310 315 320 Ala Glu Arg Ile Ser Ile Thr Asn Ile Arg Ile Ile Glu Thr Arg Glu 325 330 335 Asp Ile Asn Gly Ile Leu Arg Ile Ser Phe Gln Ser Asp Asp Asp Arg 340 345 350 Lys Arg Ala Glu Gln Cys Ile Glu Ala Arg Ala Glu Tyr Glu Thr Phe 355 360 365 Tyr Ala Asp 370 18 1122 DNA Escherichia coli CDS (1)..(1122) 18 atg gtt gct gaa ttg acc gca tta cgc gat caa att gat gaa gtc gat 48 Met Val Ala Glu Leu Thr Ala Leu Arg Asp Gln Ile Asp Glu Val Asp 1 5 10 15 aaa gcg ctg ctg aat tta tta gcg aag cgt ctg gaa ctg gtt gct gaa 96 Lys Ala Leu Leu Asn Leu Leu Ala Lys Arg Leu Glu Leu Val Ala Glu 20 25 30 gtg ggc gag gtg aaa agc cgc ttt gga ctg cct att tat gtt ccg gag 144 Val Gly Glu Val Lys Ser Arg Phe Gly Leu Pro Ile Tyr Val Pro Glu 35 40 45 cgc gag gca tct atg ttg gcc tcg cgt cgt gca gag gcg gaa gct ctg 192 Arg Glu Ala Ser Met Leu Ala Ser Arg Arg Ala Glu Ala Glu Ala Leu 50 55 60 ggt gta ccg cca gat ctg att gag gat gtt ttg cgt cgg gtg atg cgt 240 Gly Val Pro Pro Asp Leu Ile Glu Asp Val Leu Arg Arg Val Met Arg 65 70 75 80 gaa tct tac tcc agt gaa aac gac aaa gga ttt aaa aca ctt tgt ccg 288 Glu Ser Tyr Ser Ser Glu Asn Asp Lys Gly Phe Lys Thr Leu Cys Pro 85 90 95 tca ctg cgt ccg gtg gtt atc gtc ggc ggt ggc ggt cag atg gga cgc 336 Ser Leu Arg Pro Val Val Ile Val Gly Gly Gly Gly Gln Met Gly Arg 100 105 110 ctg ttc gag aag atg ctg acc ctc tcg ggt tat cag gtg cgg att ctg 384 Leu Phe Glu Lys Met Leu Thr Leu Ser Gly Tyr Gln Val Arg Ile Leu 115 120 125 gag caa cat gac tgg gat cga gcg gct gat att gtt gcc gat gcc gga 432 Glu Gln His Asp Trp Asp Arg Ala Ala Asp Ile Val Ala Asp Ala Gly 130 135 140 atg gtg att gtt agt gtg cca atc cac gtt act gag caa gtt att ggc 480 Met Val Ile Val Ser Val Pro Ile His Val Thr Glu Gln Val Ile Gly 145 150 155 160 aaa tta ccg cct tta ccg aaa gat tgt att ctg gtc gat ctg gca tca 528 Lys Leu Pro Pro Leu Pro Lys Asp Cys Ile Leu Val Asp Leu Ala Ser 165 170 175 gtg aaa aat ggg cca tta cag gcc atg ctg gtg gcg cat gat ggt ccg 576 Val Lys Asn Gly Pro Leu Gln Ala Met Leu Val Ala His Asp Gly Pro 180 185 190 gtg ctg ggg cta cac ccg atg ttc ggt ccg gac agc ggt agc ctg gca 624 Val Leu Gly Leu His Pro Met Phe Gly Pro Asp Ser Gly Ser Leu Ala 195 200 205 aag caa gtt gtg gtc tgg tgt gat gga cgt aaa ccg gaa gca tac caa 672 Lys Gln Val Val Val Trp Cys Asp Gly Arg Lys Pro Glu Ala Tyr Gln 210 215 220 tgg ttt ctg gag caa att cag gtc tgg ggc gct cgg ctg cat cgt att 720 Trp Phe Leu Glu Gln Ile Gln Val Trp Gly Ala Arg Leu His Arg Ile 225 230 235 240 agc gcc gtc gag cac gat cag aat atg gcg ttt att cag gca ctg cgc 768 Ser Ala Val Glu His Asp Gln Asn Met Ala Phe Ile Gln Ala Leu Arg 245 250 255 cac ttt gct act ttt gct tac ggg ctg cac ctg gca gaa gaa aat gtt 816 His Phe Ala Thr Phe Ala Tyr Gly Leu His Leu Ala Glu Glu Asn Val 260 265 270 cag ctt gag caa ctt ctg gcg ctc tct tcg ccg att tac cgc ctt gag 864 Gln Leu Glu Gln Leu Leu Ala Leu Ser Ser Pro Ile Tyr Arg Leu Glu 275 280 285 ctg gcg atg gtc ggg cga ctg ttt gct cag gat ccg cag ctt tat gcc 912 Leu Ala Met Val Gly Arg Leu Phe Ala Gln Asp Pro Gln Leu Tyr Ala 290 295 300 gac atc att atg tcg tca gag cgt aat ctg gcg tta atc aaa cgt tac 960 Asp Ile Ile Met Ser Ser Glu Arg Asn Leu Ala Leu Ile Lys Arg Tyr 305 310 315 320 tat aag cgt ttc ggc gag gcg att gag ttg ctg gag cag ggc gat aag 1008 Tyr Lys Arg Phe Gly Glu Ala Ile Glu Leu Leu Glu Gln Gly Asp Lys 325 330 335 cag gcg ttt att gac agt ttc cgc aag gtg gag cac tgg ttc ggc gat 1056 Gln Ala Phe Ile Asp Ser Phe Arg Lys Val Glu His Trp Phe Gly Asp 340 345 350 tac gca cag cgt ttt cag agt gaa agc cgc gtg tta ttg cgt cag gcg 1104 Tyr Ala Gln Arg Phe Gln Ser Glu Ser Arg Val Leu Leu Arg Gln Ala 355 360 365 aat gac aat cgc cag taa 1122 Asn Asp Asn Arg Gln 370 19 373 PRT Escherichia coli 19 Met Val Ala Glu Leu Thr Ala Leu Arg Asp Gln Ile Asp Glu Val Asp 1 5 10 15 Lys Ala Leu Leu Asn Leu Leu Ala Lys Arg Leu Glu Leu Val Ala Glu 20 25 30 Val Gly Glu Val Lys Ser Arg Phe Gly Leu Pro Ile Tyr Val Pro Glu 35 40 45 Arg Glu Ala Ser Met Leu Ala Ser Arg Arg Ala Glu Ala Glu Ala Leu 50 55 60 Gly Val Pro Pro Asp Leu Ile Glu Asp Val Leu Arg Arg Val Met Arg 65 70 75 80 Glu Ser Tyr Ser Ser Glu Asn Asp Lys Gly Phe Lys Thr Leu Cys Pro 85 90 95 Ser Leu Arg Pro Val Val Ile Val Gly Gly Gly Gly Gln Met Gly Arg 100 105 110 Leu Phe Glu Lys Met Leu Thr Leu Ser Gly Tyr Gln Val Arg Ile Leu 115 120 125 Glu Gln His Asp Trp Asp Arg Ala Ala Asp Ile Val Ala Asp Ala Gly 130 135 140 Met Val Ile Val Ser Val Pro Ile His Val Thr Glu Gln Val Ile Gly 145 150 155 160 Lys Leu Pro Pro Leu Pro Lys Asp Cys Ile Leu Val Asp Leu Ala Ser 165 170 175 Val Lys Asn Gly Pro Leu Gln Ala Met Leu Val Ala His Asp Gly Pro 180 185 190 Val Leu Gly Leu His Pro Met Phe Gly Pro Asp Ser Gly Ser Leu Ala 195 200 205 Lys Gln Val Val Val Trp Cys Asp Gly Arg Lys Pro Glu Ala Tyr Gln 210 215 220 Trp Phe Leu Glu Gln Ile Gln Val Trp Gly Ala Arg Leu His Arg Ile 225 230 235 240 Ser Ala Val Glu His Asp Gln Asn Met Ala Phe Ile Gln Ala Leu Arg 245 250 255 His Phe Ala Thr Phe Ala Tyr Gly Leu His Leu Ala Glu Glu Asn Val 260 265 270 Gln Leu Glu Gln Leu Leu Ala Leu Ser Ser Pro Ile Tyr Arg Leu Glu 275 280 285 Leu Ala Met Val Gly Arg Leu Phe Ala Gln Asp Pro Gln Leu Tyr Ala 290 295 300 Asp Ile Ile Met Ser Ser Glu Arg Asn Leu Ala Leu Ile Lys Arg Tyr 305 310 315 320 Tyr Lys Arg Phe Gly Glu Ala Ile Glu Leu Leu Glu Gln Gly Asp Lys 325 330 335 Gln Ala Phe Ile Asp Ser Phe Arg Lys Val Glu His Trp Phe Gly Asp 340 345 350 Tyr Ala Gln Arg Phe Gln Ser Glu Ser Arg Val Leu Leu Arg Gln Ala 355 360 365 Asn Asp Asn Arg Gln 370 20 1152 DNA Erwinia herbicola CDS (1)..(1119) 20 atg gtg gct gaa ctg acc gcg tta cgc gat caa att gac agt gta gat 48 Met Val Ala Glu Leu Thr Ala Leu Arg Asp Gln Ile Asp Ser Val Asp 1 5 10 15 aaa gcg ctg ctg gat ctg ctg gct aag cga ctg gaa ctg gtg gcc gag 96 Lys Ala Leu Leu Asp Leu Leu Ala Lys Arg Leu Glu Leu Val Ala Glu 20 25 30 gta ggt gag gtg aag agc cgt tac ggc ctg cct atc tat gtg cct gag 144 Val Gly Glu Val Lys Ser Arg Tyr Gly Leu Pro Ile Tyr Val Pro Glu 35 40 45 cgt gag gcg tcg atg ctg gct tcg cgt cgc aaa gag gcc gaa gcg ctc 192 Arg Glu Ala Ser Met Leu Ala Ser Arg Arg Lys Glu Ala Glu Ala Leu 50 55 60 ggc gta cca ccg gat ctg att gag gat gtg ctg cgt cgc gtg atg cgg 240 Gly Val Pro Pro Asp Leu Ile Glu Asp Val Leu Arg Arg Val Met Arg 65 70 75 80 gaa tcc tat acc agc gag aat gat aaa ggc ttt aaa acc ctc tgt cct 288 Glu Ser Tyr Thr Ser Glu Asn Asp Lys Gly Phe Lys Thr Leu Cys Pro 85 90 95 gaa ctg cgc ccg gtg gtg att gtc ggt ggt aag ggc cag atg ggc cgg 336 Glu Leu Arg Pro Val Val Ile Val Gly Gly Lys Gly Gln Met Gly Arg 100 105 110 ctg ttt gaa aaa atg ctc ggg cta tca ggc tac acg gtt aaa acg ctg 384 Leu Phe Glu Lys Met Leu Gly Leu Ser Gly Tyr Thr Val Lys Thr Leu 115 120 125 gat aaa gag gac tgg cct cag gct gag act ctg ctc agc gat gcc gga 432 Asp Lys Glu Asp Trp Pro Gln Ala Glu Thr Leu Leu Ser Asp Ala Gly 130 135 140 atg gtg atc att agc gtg ccg att cac ctg acc gag cag gtg att gcc 480 Met Val Ile Ile Ser Val Pro Ile His Leu Thr Glu Gln Val Ile Ala 145 150 155 160 caa ctg cca cca ctg ccg gaa gat tgt att ctg gtc gat ctg gcg tca 528 Gln Leu Pro Pro Leu Pro Glu Asp Cys Ile Leu Val Asp Leu Ala Ser 165 170 175 gtc aaa aac cgg cct ctg cag gca atg ctg gct gcc cat aac ggg cct 576 Val Lys Asn Arg Pro Leu Gln Ala Met Leu Ala Ala His Asn Gly Pro 180 185 190 gta ctg ggt ctg cat ccg atg ttt ggc ccg gac agc ggc agc ctg gca 624 Val Leu Gly Leu His Pro Met Phe Gly Pro Asp Ser Gly Ser Leu Ala 195 200 205 aaa cag gtg gtg gtc tgg tgt gat gga aga caa ccg gaa gcg tat cag 672 Lys Gln Val Val Val Trp Cys Asp Gly Arg Gln Pro Glu Ala Tyr Gln 210 215 220 tgg ttc ctg gag cag att cag gtc tgg ggt gcg cgt ctg cat cgt atc 720 Trp Phe Leu Glu Gln Ile Gln Val Trp Gly Ala Arg Leu His Arg Ile 225 230 235 240 agc gct gtt gag cat gac cag aac atg gca ttc att cag gcg ctg cgt 768 Ser Ala Val Glu His Asp Gln Asn Met Ala Phe Ile Gln Ala Leu Arg 245 250 255 cac ttt gct acc ttc gct tat ggt ctg cat tta gcc gaa gag aac gtc 816 His Phe Ala Thr Phe Ala Tyr Gly Leu His Leu Ala Glu Glu Asn Val 260 265 270 aat ctg gat cag ctg ctg gcg ctc tcg tcg ccc att tac cgg ctt gaa 864 Asn Leu Asp Gln Leu Leu Ala Leu Ser Ser Pro Ile Tyr Arg Leu Glu 275 280 285 ctg gcg atg gtg ggg cgg ttg ttc gct cag gat ccg caa ctc tat gcg 912 Leu Ala Met Val Gly Arg Leu Phe Ala Gln Asp Pro Gln Leu Tyr Ala 290 295 300 gat atc atc atg tct tca gag agt aat ctg gcg ctg ata aaa cgc tat 960 Asp Ile Ile Met Ser Ser Glu Ser Asn Leu Ala Leu Ile Lys Arg Tyr 305 310 315 320 tac cag cgg ttt ggt gaa gcg att gcg ctg ctg gag cag ggc gac aag 1008 Tyr Gln Arg Phe Gly Glu Ala Ile Ala Leu Leu Glu Gln Gly Asp Lys 325 330 335 cag gcg ttt atc gcc agc ttt aac cgg gtt gaa cag tgg ttt ggc gat 1056 Gln Ala Phe Ile Ala Ser Phe Asn Arg Val Glu Gln Trp Phe Gly Asp 340 345 350 cac gca aaa cgc ttc ctg gtc gaa agc cga agc ctg ttg cga tcg gcc 1104 His Ala Lys Arg Phe Leu Val Glu Ser Arg Ser Leu Leu Arg Ser Ala 355 360 365 aat gac agc cgc cca taaaaaaaag gcatccagtt ggatgccttt ttt 1152 Asn Asp Ser Arg Pro 370 21 373 PRT Erwinia herbicola 21 Met Val Ala Glu Leu Thr Ala Leu Arg Asp Gln Ile Asp Ser Val Asp 1 5 10 15 Lys Ala Leu Leu Asp Leu Leu Ala Lys Arg Leu Glu Leu Val Ala Glu 20 25 30 Val Gly Glu Val Lys Ser Arg Tyr Gly Leu Pro Ile Tyr Val Pro Glu 35 40 45 Arg Glu Ala Ser Met Leu Ala Ser Arg Arg Lys Glu Ala Glu Ala Leu 50 55 60 Gly Val Pro Pro Asp Leu Ile Glu Asp Val Leu Arg Arg Val Met Arg 65 70 75 80 Glu Ser Tyr Thr Ser Glu Asn Asp Lys Gly Phe Lys Thr Leu Cys Pro 85 90 95 Glu Leu Arg Pro Val Val Ile Val Gly Gly Lys Gly Gln Met Gly Arg 100 105 110 Leu Phe Glu Lys Met Leu Gly Leu Ser Gly Tyr Thr Val Lys Thr Leu 115 120 125 Asp Lys Glu Asp Trp Pro Gln Ala Glu Thr Leu Leu Ser Asp Ala Gly 130 135 140 Met Val Ile Ile Ser Val Pro Ile His Leu Thr Glu Gln Val Ile Ala 145 150 155 160 Gln Leu Pro Pro Leu Pro Glu Asp Cys Ile Leu Val Asp Leu Ala Ser 165 170 175 Val Lys Asn Arg Pro Leu Gln Ala Met Leu Ala Ala His Asn Gly Pro 180 185 190 Val Leu Gly Leu His Pro Met Phe Gly Pro Asp Ser Gly Ser Leu Ala 195 200 205 Lys Gln Val Val Val Trp Cys Asp Gly Arg Gln Pro Glu Ala Tyr Gln 210 215 220 Trp Phe Leu Glu Gln Ile Gln Val Trp Gly Ala Arg Leu His Arg Ile 225 230 235 240 Ser Ala Val Glu His Asp Gln Asn Met Ala Phe Ile Gln Ala Leu Arg 245 250 255 His Phe Ala Thr Phe Ala Tyr Gly Leu His Leu Ala Glu Glu Asn Val 260 265 270 Asn Leu Asp Gln Leu Leu Ala Leu Ser Ser Pro Ile Tyr Arg Leu Glu 275 280 285 Leu Ala Met Val Gly Arg Leu Phe Ala Gln Asp Pro Gln Leu Tyr Ala 290 295 300 Asp Ile Ile Met Ser Ser Glu Ser Asn Leu Ala Leu Ile Lys Arg Tyr 305 310 315 320 Tyr Gln Arg Phe Gly Glu Ala Ile Ala Leu Leu Glu Gln Gly Asp Lys 325 330 335 Gln Ala Phe Ile Ala Ser Phe Asn Arg Val Glu Gln Trp Phe Gly Asp 340 345 350 His Ala Lys Arg Phe Leu Val Glu Ser Arg Ser Leu Leu Arg Ser Ala 355 360 365 Asn Asp Ser Arg Pro 370 22 1129 DNA Lycopersicon esculentum 22 atgttttccc tttcatctat acaatctaac aatattcaat ctcaatcatc ttcgtcgcta 60 ctcttcaatc atcatcacca gcattcaact atttcaactc ggtttcatca ccaccgccta 120 ctcttccctc tccgtgccca aaatagcgac ttaactacag ccaccaccaa taacaactat 180 gtcgatcttg atgacaatct aaccagactt gataaatttt caaaatcatt aagtatttcg 240 aatatcgaag aaaatacatc attaaatccc ctcttatgtt ccaataacaa gctcaaaata 300 gctatcatag gctttggaaa ctttggacaa tttattgcca aatcctttat caaacaaggc 360 catgttgtat tagctcattc acgtagtgat tattccctca tagcacaatc ccttaatgtc 420 cacttctttc aagatcctaa tgacttatgt gaacaacatc ctgacgttat tttactttgc 480 acatccatca attcactcga aaacgtcatt cgttcccttc ccatccaaaa gcttaaacgt 540 aacacacttt tcgtagacgt attatcagtc aaagaattcc cgaaaaacat ttttcttcaa 600 tcactaccaa aagaatttga tattttgtgt actcatccta tgtttggtcc aacaagtggt 660 aaagacaatt ggaaaggact accatttatg tatgacaaag ttagaattgg acaagaagag 720 tcaagaatta aaagagtcaa caattttatc aacatttttg taaaagaagg ttgtagaatg 780 gttgaaatga gttgtagtga acatgacaag tatgctgctg gatcacaatt tattacacat 840 actattggaa gaatgttaca aagacttggg acacaaacaa ctcctataaa cacaaaagga 900 tatgaaagtt tgttgaattt gatggagaat acaactagtg atagttttga tttgtattgt 960 ggtttgctta tgtataacaa taattcaatg gaggtgttag agaaactaga tgcagcattg 1020 gatagtttga aaagggaatt atttggacaa gttcttcaaa agttggagaa aagagtggaa 1080 aagggaagta agttagcttt acctactcct gattttagta agaaaattg 1129 23 32 DNA Artificial Oligonucleotide P1 23 tctccatatg atctttcaat ctcattctca tc 32 24 32 DNA Artificial Oligonucleotide P2 24 ctaactaact aactacatac ctcatcatat cc 32 25 26 DNA Artificial Oligonucleotide P3 25 cctctctttc catatgctcc cttctc 26 26 33 DNA Artificial Oligonucleotide P4 26 ccgccagcca cctccatatg accgacacca tcc 33 27 25 DNA Artificial Oligonucleotide P5 27 cgccacccct catatgcgta tcgcc 25 28 34 DNA Artificial Oligonucleotide P6 28 gatgcatctt tgcatatgat gaggtcagaa gatg 34 29 35 DNA Artificial Oligonucleotide P7 29 cagtataatt agtagtcaag gatcctgact gagag 35 30 31 DNA Artificial Oligonucleotide P8 30 gctaaaactc ttctccttca atacttacct g 31 

1. An isolated polynucleotide encoding an enzyme having arogenate dehydrogenase activity.
 2. The polynucleotide as claimed in claim 1, characterized in that it comprises a polynucleotide selected from the group consisting of: (a) an isolated polynucleotide encoding the polypeptide described by the sequence identifier SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7 or SEQ ID NO: 9; (b) an isolated polynucleotide which hybridizes to the polynucleotide according to (a); (c) an isolated polynucleotide homologous to a polynucleotide according to (a) or (b); (d) a fragment of a polynucleotide according to (a), (b) or (c).
 3. The polynucleotide as claimed in claim 2, characterized in that it comprises a polynucleotide selected from the sequence identifiers SEQ ID NO: 1, SEQ ID NO:
 2. SEQ ID NO: 4, SEQ ID NO: 6 or SEQ ID NO:
 8. 4. The polynucleotide as claimed in claim 1, characterized in that it comprises a polynucleotide selected from the group consisting of: (a) an isolated polynucleotide encoding the polypeptide described by the sequence identifier SEQ ID NO: 11; (b) an isolated polynucleotide which hybridizes to the polynucleotide according to (a); (c) an isolated polynucleotide homologous to a polynucleotide according to (a) or (b); (d) a fragment of a polynucleotide according to (a), (b) or (c).
 5. The polynucleotide as claimed in claim 4, characterized in that it comprises a polynucleotide selected from the sequence identifiers SEQ ID NO:
 10. 6. The isolated polynucleotide as claimed in one of claims 1 to 5, characterized in that it originates from plants.
 7. The isolated polynucleotide as claimed in claim 3, characterized in that it originates from Arabidopsis thaliana.
 8. The isolated polynucleotide as claimed in claim 5, characterized in that it originates from Picea glauca.
 9. The polynucleotide as claimed in claim 1, characterized in that it comprises a polynucleotide selected from the group consisting of: (a) an isolated polynucleotide encoding the polypeptide described by the sequence identifier SEQ ID NO: 13; (b) an isolated polynucleotide which hybridizes to the polynucleotide according to (a); (c) an isolated polynucleotide homologous to a polynucleotide according to (a) or (b); (d) a fragment of a polynucleotide according to (a), (b) or (c).
 10. The polynucleotide as claimed in claim 9, characterized in that it comprises a polynucleoltide selected from the sequence identifiers SEQ ID NO:
 11. 11. The isolated polynucleotide as claimed in either of claims 9 and 10, characterized in that it originates from a bacterium.
 12. The isolated polynucleotide as claimed in claim 11, characterized in that it originates from a bacterium of the Synechocystis genus.
 13. An enzyme with arogenate dehydrogenase activity, characterized in that it is encoded by a polynucleotide as claimed in one of claims 1 to
 8. 14. The enzyme with arogenate dehydrogenase activity as claimed in claim 13, characterized in that it originates from a plant.
 15. An enzyme with arogenate dehydrogenase activity, characterized in that it is encoded by a polynucleotide as claimed in one of claims 9 to
 12. 16. The enzyme with arogenate dehydrogenase activity as claimed in claim 15, characterized in that it originates from a bacterium.
 17. A chimeric gene comprising, functionally linked to one another, at least: (a) one promoter which is functional in a host organism; (b) a polynucleotide as claimed in one of claims 1 to 12; (c) a terminator element which is functional in a host organism.
 18. The chimeric gene as claimed in claim 17, characterized in that the promoter is a constitutive promoter.
 19. The chimeric gene as claimed in claim 17, characterized in that the promoter is a inducible promoter.
 20. The chimeric gene as claimed in one of claims 17 to 19, characterized in that it also comprises a signal peptide or a transit peptide which is functional in said host organism.
 21. The chimeric gene as claimed in one of claims 17 to 20, characterized in that the host organism is a microorganism.
 22. The chimeric gene as claimed in one of claims 17 to 20, characterized in that the host organism is a plant cell or a plant.
 23. An expression or transformation vector containing a chimeric gene as claimed in one of claims 17 to
 22. 24. The vector as claimed in claim 23, characterized in that it is a plasmid, a phage or a virus.
 25. A host organism transformed with one of the vectors as claimed in either of claims 23 and
 24. 26. The host organism as claimed in claim 25, characterized in that it is a microorganism.
 27. The host organism as claimed in claim 26, characterized in that the microorganism is a bacterium of the species Escherichia coli.
 28. The host organism as claimed in claim 26, characterized in that the microorganism is a yeast of the Saccharomyces, Kluyveromyces or Pichia genus.
 29. The host organism as claimed in claim 26, characterized in that the microorganism is a baculovirus.
 30. A transformed plant cell containing a chimeric gene as claimed in one of claims 17 to
 22. 31. A method for preparing arogenate dehydrogenase enzyme, characterized in that (a) a transformed organism or plant cell as claimed in one of claims 25 to 30 is cultured in a suitable culture medium; (b) the arogenate dehydrogenase enzyme produced is recovered from the culture medium by centrifugation or by filtration; (c) the enzyme recovered in step (b) is purified by passing it through at least one chromatography column.
 32. A method for identifying a herbicidal compound having as a target an enzyme with arogenate dehydrogenase activity, characterized in that (a) at least two samples, each containing an equivalent amount of an arogenate dehydrogenase enzyme in solution, are prepared; (b) one of the samples is treated with a compound; (c) the arogenate dehydrogenase activity is measured in each one of said samples; (d) the compound used in step (b) is identified as being a herbicidal compound when the activity measured in step (c) is significantly less in the treated sample compared to the untreated sample; (e) the herbicidal activity of the compound identified in step (d) is validated by treating plants with said compound.
 33. The method as claimed in claim 32, characterized in that the enzyme with arogenate dehydrogenase activity used in step (a) is an enzyme as claimed in one of claims 13 to
 16. 34. A herbicidal compound, characterized in that it has as a target an arogenate dehydrogenase enzyme.
 35. The herbicidal compound as claimed in claim 34, characterized in that it has as a target an arogenate dehydrogenase enzyme as claimed in one of claims 13 to
 16. 36. The herbicidal compound as claimed in either of claims 34 and 35, characterized in that it is obtained using the method as claimed in either of claims 32 and
 33. 37. A plant tolerant with respect to a herbicidal compound having as a target an enzyme involved in one of the metabolic steps for conversion of prephenate to L-tyrosine, characterized in that it contains a gene encoding a prephenate dehydrogenase enzyme and expresses said enzyme in its tissues.
 38. The plant as claimed in claim 37, characterized in that it is tolerant with respect to a herbicidal compound having as a target an arogenate dehydrogenase enzyme.
 39. The plant as claimed in claim 38, characterized in that it is tolerant with respect to a herbicidal compound as claimed in one of claims 34 to
 36. 40. The plant as claimed in claim 37, characterized in that it is tolerant with respect to a herbicidal compound having as a target a prephenate aminotransferase enzyme.
 41. The tolerant plants as claimed in one of claims 37 to 40, characterized in that the gene encoding a prephenate dehydrogenase enzyme is a yeast gene.
 42. The tolerant plant as claimed in claim 41, characterized in that the gene encoding a prephenate dehydrogenase enzyme originates from a yeast of the Saccharomyces genus.
 43. The tolerant plant as claimed in claim 42, characterized in that the gene encoding a prephenate dehydrogenase enzyme is represented by the sequence identifier SEQ ID NO:
 14. 44. The tolerant plant as claimed in one of claims 37 to 40, characterized in that the gene encoding a prephenate dehydrogenase enzyme originates from a bacterium.
 45. The tolerant plant as claimed in claim 44, characterized in that the gene encoding a prephenate dehydrogenase enzyme originates from a bacterium of the Bacillus genus.
 46. The tolerant plant as claimed in claim 45, characterized in that the gene encoding a prephenate dehydrogenase enzyme is represented by the sequence identifier SEQ ID NO:
 16. 47. The tolerant plant as claimed in claim 44, characterized in that the gene encoding a prephenate dehydrogenase enzyme originates from a bacterium of the Escherichia genus.
 48. The tolerant plant as claimed in claim 47, characterized in that the gene encoding a prephenate dehydrogenase enzyme is represented by the sequence identifier SEQ ID NO:
 18. 49. The tolerant plant as claimed in claim 44, characterized in that the gene encoding a prephenate dehydrogenase enzyme originates from a bacterium of the Erwinia genus.
 50. The tolerant plant as claimed in claim 49, characterized in that the gene encoding a prephenate dehydrogenase enzyme is represented by the sequence identifier SEQ ID NO:
 20. 51. A method for producing plants tolerant with respect to herbidical compounds having as a target an enzyme involved in one of the metabolic steps for conversion of prephenate to L-tyrosine, characterized in that said plants are transformed with a gene encoding a prephenate dehydrogenase enzyme in such a way that they express it in their tissues.
 52. The method as claimed in claim 51, characterized in that it applies to the production of plants tolerant with respect to herbicidal compounds having as a target the arogenate dehydrogenase enzyme.
 53. The method as claimed in claim 51, characterized in that it applies to the production of plants tolerant with respect to herbicidal compounds having as a target the prephenate aminotransferase enzyme.
 54. The method as claimed in one of claims 51 to 53, characterized in that the prephenate dehydrogenase enzyme originates from a yeast.
 55. The method as claimed in one of claims 51 to 53, characterized in that the prephenate dehydrogenase enzyme originates from a fungus.
 56. The method as claimed in one of claims 51 to 53, characterized in that the prephenate dehydrogenase enzyme originates from a bacterium.
 57. The tolerant plant as claimed in one of claims 37 to 50, characterized in that it contains, in addition to a chimeric gene as claimed in one of claims 17 to 22, at least one other gene containing a polynucleotide encoding a protein of interest. 